Proteopedia - User contributions [en]

Sandbox Reserved 1567

2019-12-09T03:38:16Z

Deja Sanders:

==Tetrahydroprotoberbine N-methyltransferase==
= Structure =
<StructureSection load='6P3N' size='340' side='right' caption='Tetrahydroprotoberbine' scene=''>
'''Tetrahydroprotoberbine N-methyltransferase''' is a protein thats dimer interface includes six salt 6 salt bridges and 8 hydrogens bonds. It is expressed in E. ''coli'' and crystallized at a pH of 7.0. The crystals were grown in the presence of SAH,SAM, and SAH+SMS. The most significant substrate is SAM which is shown to the right.

= Function =
The protein being studied, Tetrahydroprotoberbine N-methyltransferase, is found in yellow horned poppy (''Glaucium Flavum''). The function of the protein is substate recognition as well as catalysis for the ration engineering of enyzmes for chemoenzymatic synthesis and metabolic engineering. The relative activity of about 8 substrates were tested wiht Protoberberine having the highest percentage. GfTNMT's activity depends on temperature and pH. When the enzyme's activity was at a pH of 8, dropped 10% in activity. 10% activity was also dropped when the temperature was at 30 degrees Celsius. When at 4 degrees Celsius, the activity dropped even more down to 40%. <ref>Liscombe, D. K., and Facchini, P. J. (2007) Molecular cloning and characterization of tetrahydroprotoberberine cis-N-methyltransferase, an enzyme involved in alkaloid biosynthesis in opium poppy. J. Biol. Chem. 282,14741–14751 CrossRef Medline</ref>
= Mutants =
In TMNT, three amino acid residues in the alpha14-helix form one side of the <scene name='82/829888/Binding_pocket/1'>binding pocket</scene> defining the BP region. The binding pocket consists of His-328(green), Ile-329(purple), and Phe-332(orange). The H328 mutation decreases in activity with stylopine and scoulerine producing a 5- and 2-fold while the activity with THP increases 2-fold.
= Relevance =
Studying Tetrahydroprotoberbine will provide commercial application where one will gain a lot of knowledge from both the research paper and online sources. Studying this protein will allow readers to engage in the material and apply their own knowledge to better understand the study. This research will provide descriptive roles that TNMT plays such as pathway leading to the formation of different substrates including Protoberberine. <ref> Takao, N., Kamigauchi, M., and Okada, M. (1983) Biosynthesis of benzo-[c]phenanthridine alkaloids sanguinarine, chelirubine and macarpine.Helv. Chim. Acta 66, 473–484 CrossRef </ref>
= Structural Highlights =
This protein has a <scene name='82/829888/Catalytic_triad/9'>catalytic triad</scene> which consists of amino acids His-208(pink), Glu-204(blue), and Glu-207(yellow). The catalytic triad are the three amino acids present in the active site involved in catalysis The authors explained within the paper that other amino acids may play a role in the triad as well. They were unsure but those three were the most accurate. These amino acids play an important role in catalysis for the protein. <ref> Bennett, M. R., Thompson, M. L., Shepherd, S. A., Dunstan, M. S., Herbert, A. J., Smith, D. R. M., Cronin, V. A., Menon, B. R. K., Levy, C., and Micklefield, J. (2018) Structure and biocatalytic scope of coclaurine Nmethyltransferase.Angew. Chem. Int. Ed. Engl. 57, 10600–10604CrossRef
Medline </ref>. The basic <scene name='82/829888/Spacefill_view_of_protein/1'>spacefill view</scene> of the entire protein alllows readers to visualize the different elements show in different colors. The elements shown are carbons(grey), nitrogen(blue), and oxygen(red). This protein has a <scene name='82/829888/Ligand/1'>ligand</scene> which is SAM. There are <scene name='82/829888/Hydrophilic_side_chains/1'>hydrophilic side chains</scene> of SAM that form a small catalytic pocket and surrounds the amino group and methyl donor of SAM. This catalytic pocket forms a L shape. In green Glu-204, yellow is Glu-207, red is His-208, and Tyr-81 is blue. There are <scene name='82/823091/Hydrophobic_side_chains/1'>hydrophobic side chains</scene> that consist of Ile-234(purple), Phe-243(green), Phe-257(yellow), Val-262(blue), Met-290(red),and Phe-340(baby blue) which form a isoquinoline pocket. The <scene name='82/829888/Active_site/3'>active site</scene> of the protein consists of amino acids Valine-188(yellow), Aspartic Acid-187(blue), and Alanine-186(green), with purple being the rest of the ligand, SAM. The active site is the region where substrate molecules bind and undergo a chemical reaction. The <scene name='82/829888/Secondary_structure/1'>secondary structure</scene> of this protein contains a pattern of hydrogen bonds between atoms in the peptide bond. This cartoon view allows readers to visualize the alpha(pink) and beta sheets(yellow). The protein consists of two regions which are <scene name='82/829888/Polar_and_non-polar/1'>polar and non-polar regions</scene>. The non-polar region is in grey while the polar region is in purple. The <scene name='82/829888/Cationic_region/1'>cationic region</scene> of the protein has a side chain of Lysine, Arginine, Aspartic Acid, and Glutamic Acid. The cationic region is in the light blue.

= Energy Transformation =
The exact values for kinetic parameters are challenging to determine because of the presence of high levels of apparent substrate and product inhibition. <ref> Liscombe, D. K., Ziegler, J., Schmidt, J., Ammer, C., and Facchini, P.J.
(2009) Targeted metabolite and transcript profiling for elucidating enzyme function: isolation of novel N-methyltransferases from three benzylisoquinoli </ref>
</StructureSection>
== References ==
<references/>

Sandbox Reserved 1567

2019-12-09T03:29:58Z

Deja Sanders:

==Tetrahydroprotoberbine N-methyltransferase==
= Structure =
<StructureSection load='6P3N' size='340' side='right' caption='Tetrahydroprotoberbine' scene=''>
'''Tetrahydroprotoberbine N-methyltransferase''' is a protein thats dimer interface includes six salt 6 salt bridges and 8 hydrogens bonds. It is expressed in E. ''coli'' and crystallized at a pH of 7.0. The crystals were grown in the presence of SAH,SAM, and SAH+SMS. The most significant substrate is SAM which is shown to the right.

= Function =
The protein being studied, Tetrahydroprotoberbine N-methyltransferase, is found in yellow horned poppy (''Glaucium Flavum''). The function of the protein is substate recognition as well as catalysis for the ration engineering of enyzmes for chemoenzymatic synthesis and metabolic engineering. The relative activity of about 8 substrates were tested wiht Protoberberine having the highest percentage. GfTNMT's activity depends on temperature and pH. When the enzyme's activity was at a pH of 8, dropped 10% in activity. 10% activity was also dropped when the temperature was at 30 degrees Celsius. When at 4 degrees Celsius, the activity dropped even more down to 40%. <ref>Liscombe, D. K., and Facchini, P. J. (2007) Molecular cloning and characterization of tetrahydroprotoberberine cis-N-methyltransferase, an enzyme involved in alkaloid biosynthesis in opium poppy. J. Biol. Chem. 282,14741–14751 CrossRef Medline</ref>
= Mutants =
In TMNT, three amino acid residues in the alpha14-helix form one side of the <scene name='82/829888/Binding_pocket/1'>binding pocket</scene> defining the BP region. The binding pocket consists of His-328(green), Ile-329(purple), and Phe-332(orange). The H328 mutation decreases in activity with stylopine and scoulerine producing a 5- and 2-fold while the activity with THP increases 2-fold.
= Relevance =
Studying Tetrahydroprotoberbine will provide commercial application where one will gain a lot of knowledge from both the research paper and online sources. Studying this protein will allow readers to engage in the material and apply their own knowledge to better understand the study. This research will provide descriptive roles that TNMT plays such as pathway leading to the formation of different substrates including Protoberberine. <ref> Takao, N., Kamigauchi, M., and Okada, M. (1983) Biosynthesis of benzo-[c]phenanthridine alkaloids sanguinarine, chelirubine and macarpine.Helv. Chim. Acta 66, 473–484 CrossRef </ref>
= Structural Highlights =
This protein has a <scene name='82/829888/Catalytic_triad/7'>catalytic triad</scene> which consists of amino acids His-208(pink), Glu-204(blue), and Glu-207(yellow). The catalytic triad are the three amino acids present in the active site involved in catalysis The authors explained within the paper that other amino acids may play a role in the triad as well. They were unsure but those three were the most accurate. These amino acids play an important role in catalysis for the protein. <ref> Bennett, M. R., Thompson, M. L., Shepherd, S. A., Dunstan, M. S., Herbert, A. J., Smith, D. R. M., Cronin, V. A., Menon, B. R. K., Levy, C., and Micklefield, J. (2018) Structure and biocatalytic scope of coclaurine Nmethyltransferase.Angew. Chem. Int. Ed. Engl. 57, 10600–10604CrossRef
Medline </ref>. The basic <scene name='82/829888/Spacefill_view_of_protein/1'>spacefill view</scene> of the entire protein alllows readers to visualize the different elements show in different colors. The elements shown are carbons(grey), nitrogen(blue), and oxygen(red). This protein has a <scene name='82/829888/Ligand/1'>ligand</scene> which is SAM. There are <scene name='82/829888/Hydrophilic_side_chains/1'>hydrophilic side chains</scene> of SAM that form a small catalytic pocket and surrounds the amino group and methyl donor of SAM. This catalytic pocket forms a L shape. In green Glu-204, yellow is Glu-207, red is His-208, and Tyr-81 is blue. There are <scene name='82/823091/Hydrophobic_side_chains/1'>hydrophobic side chains</scene> that consist of Ile-234(purple), Phe-243(green), Phe-257(yellow), Val-262(blue), Met-290(red),and Phe-340(baby blue) which form a isoquinoline pocket. The <scene name='82/829888/Active_site/3'>active site</scene> of the protein consists of amino acids Valine-188(yellow), Aspartic Acid-187(blue), and Alanine-186(green), with purple being the rest of the ligand, SAM. The active site is the region where substrate molecules bind and undergo a chemical reaction. The <scene name='82/829888/Secondary_structure/1'>secondary structure</scene> of this protein contains a pattern of hydrogen bonds between atoms in the peptide bond. This cartoon view allows readers to visualize the alpha(pink) and beta sheets(yellow). The protein consists of two regions which are <scene name='82/829888/Polar_and_non-polar/1'>polar and non-polar regions</scene>. The non-polar region is in grey while the polar region is in purple. The <scene name='82/829888/Cationic_region/1'>cationic region</scene> of the protein has a side chain of Lysine, Arginine, Aspartic Acid, and Glutamic Acid. The cationic region is in the light blue.

= Energy Transformation =
The exact values for kinetic parameters are challenging to determine because of the presence of high levels of apparent substrate and product inhibition. <ref> Liscombe, D. K., Ziegler, J., Schmidt, J., Ammer, C., and Facchini, P.J.
(2009) Targeted metabolite and transcript profiling for elucidating enzyme function: isolation of novel N-methyltransferases from three benzylisoquinoli </ref>
</StructureSection>
== References ==
<references/>

Sandbox Reserved 1567

2019-12-09T03:27:32Z

Deja Sanders:

==Tetrahydroprotoberbine N-methyltransferase==
= Structure =
<StructureSection load='6P3N' size='340' side='right' caption='Tetrahydroprotoberbine' scene=''>
'''Tetrahydroprotoberbine N-methyltransferase''' is a protein thats dimer interface includes six salt 6 salt bridges and 8 hydrogens bonds. It is expressed in E. ''coli'' and crystallized at a pH of 7.0. The crystals were grown in the presence of SAH,SAM, and SAH+SMS. The most significant substrate is SAM which is shown to the right.

= Function =
The protein being studied, Tetrahydroprotoberbine N-methyltransferase, is found in yellow horned poppy (''Glaucium Flavum''). The function of the protein is substate recognition as well as catalysis for the ration engineering of enyzmes for chemoenzymatic synthesis and metabolic engineering. The relative activity of about 8 substrates were tested wiht Protoberberine having the highest percentage. GfTNMT's activity depends on temperature and pH. When the enzyme's activity was at a pH of 8, dropped 10% in activity. 10% activity was also dropped when the temperature was at 30 degrees Celsius. When at 4 degrees Celsius, the activity dropped even more down to 40%. <ref>Liscombe, D. K., and Facchini, P. J. (2007) Molecular cloning and characterization of tetrahydroprotoberberine cis-N-methyltransferase, an enzyme involved in alkaloid biosynthesis in opium poppy. J. Biol. Chem. 282,14741–14751 CrossRef Medline</ref>
= Mutants =
In TMNT, three amino acid residues in the alpha14-helix form one side of the <scene name='82/829888/Binding_pocket/1'>binding pocket</scene> defining the BP region. The binding pocket consists of His-328(green), Ile-329(purple), and Phe-332(orange). The H328 mutation decreases in activity with stylopine and scoulerine producing a 5- and 2-fold while the activity with THP increases 2-fold.
= Relevance =
Studying Tetrahydroprotoberbine will provide commercial application where one will gain a lot of knowledge from both the research paper and online sources. Studying this protein will allow readers to engage in the material and apply their own knowledge to better understand the study. This research will provide descriptive roles that TNMT plays such as pathway leading to the formation of different substrates including Protoberberine. <ref> Takao, N., Kamigauchi, M., and Okada, M. (1983) Biosynthesis of benzo-[c]phenanthridine alkaloids sanguinarine, chelirubine and macarpine.Helv. Chim. Acta 66, 473–484 CrossRef </ref>
= Structural Highlights =
This protein has a <scene name='82/829888/Catalytic_triad/7'>catalytic triad</scene> which consists of amino acids His-208(pink), Glu-204(blue), and Glu-207(yellow). The authors explained within the paper that other amino acids may play a role in the triad as well. They were unsure but those three were the most accurate. These amino acids play an important role in catalysis for the protein. <ref> Bennett, M. R., Thompson, M. L., Shepherd, S. A., Dunstan, M. S., Herbert, A. J., Smith, D. R. M., Cronin, V. A., Menon, B. R. K., Levy, C., and Micklefield, J. (2018) Structure and biocatalytic scope of coclaurine Nmethyltransferase.Angew. Chem. Int. Ed. Engl. 57, 10600–10604CrossRef
Medline </ref>. The basic <scene name='82/829888/Spacefill_view_of_protein/1'>spacefill view</scene> of the entire protein alllows readers to visualize the different elements show in different colors. The elements shown are carbons(grey), nitrogen(blue), and oxygen(red). This protein has a <scene name='82/829888/Ligand/1'>ligand</scene> which is SAM. There are <scene name='82/829888/Hydrophilic_side_chains/1'>hydrophilic side chains</scene> of SAM that form a small catalytic pocket and surrounds the amino group and methyl donor of SAM. This catalytic pocket forms a L shape. In green Glu-204, yellow is Glu-207, red is His-208, and Tyr-81 is blue. There are <scene name='82/823091/Hydrophobic_side_chains/1'>hydrophobic side chains</scene> that consist of Ile-234(purple), Phe-243(green), Phe-257(yellow), Val-262(blue), Met-290(red),and Phe-340(baby blue) which form a isoquinoline pocket. The <scene name='82/829888/Active_site/3'>active site</scene> of the protein consists of amino acids Valine-188(yellow), Aspartic Acid-187(blue), and Alanine-186(green), with purple being the rest of the ligand, SAM. The active site is the region where substrate molecules bind and undergo a chemical reaction. The <scene name='82/829888/Secondary_structure/1'>secondary structure</scene> of this protein contains a pattern of hydrogen bonds between atoms in the peptide bond. This cartoon view allows readers to visualize the alpha(pink) and beta sheets(yellow). The protein consists of two regions which are <scene name='82/829888/Polar_and_non-polar/1'>polar and non-polar regions</scene>. The non-polar region is in grey while the polar region is in purple. The <scene name='82/829888/Cationic_region/1'>cationic region</scene> of the protein has a side chain of Lysine, Arginine, Aspartic Acid, and Glutamic Acid. The cationic region is in the light blue.

= Energy Transformation =
The exact values for kinetic parameters are challenging to determine because of the presence of high levels of apparent substrate and product inhibition. <ref> Liscombe, D. K., Ziegler, J., Schmidt, J., Ammer, C., and Facchini, P.J.
(2009) Targeted metabolite and transcript profiling for elucidating enzyme function: isolation of novel N-methyltransferases from three benzylisoquinoli </ref>
</StructureSection>
== References ==
<references/>

Sandbox Reserved 1567

2019-12-09T01:27:50Z

Deja Sanders:

==Tetrahydroprotoberbine N-methyltransferase==
= Structure =
<StructureSection load='6P3N' size='340' side='right' caption='Tetrahydroprotoberbine' scene=''>
'''Tetrahydroprotoberbine N-methyltransferase''' is a protein thats dimer interface includes six salt 6 salt bridges and 8 hydrogens bonds. It is expressed in E. ''coli'' and crystallized at a pH of 7.0. The crystals were grown in the presence of SAH,SAM, and SAH+SMS. The most significant substrate is SAM which is shown to the right.

= Function =
The protein being studied, Tetrahydroprotoberbine N-methyltransferase, is found in yellow horned poppy (''Glaucium Flavum''). The function of the protein is substate recognition as well as catalysis for the ration engineering of enyzmes for chemoenzymatic synthesis and metabolic engineering. The relative activity of about 8 substrates were tested wiht Protoberberine having the highest percentage. GfTNMT's activity depends on temperature and pH. When the enzyme's activity was at a pH of 8, dropped 10% in activity. 10% activity was also dropped when the temperature was at 30 degrees Celsius. When at 4 degrees Celsius, the activity dropped even more down to 40%. <ref>Liscombe, D. K., and Facchini, P. J. (2007) Molecular cloning and characterization of tetrahydroprotoberberine cis-N-methyltransferase, an enzyme involved in alkaloid biosynthesis in opium poppy. J. Biol. Chem. 282,14741–14751 CrossRef Medline</ref>
= Mutants =
In TMNT, three amino acid residues in the alpha14-helix form one side of the <scene name='82/829888/Binding_pocket/1'>binding pocket</scene> defining the BP region. The binding pocket consists of His-328(green), Ile-329(purple), and Phe-332(orange). The H328 mutation decreases in activity with stylopine and scoulerine producing a 5- and 2-fold while the activity with THP increases 2-fold.
= Relevance =
Studying Tetrahydroprotoberbine will provide commercial application where one will gain a lot of knowledge from both the research paper and online sources. Studying this protein will allow readers to engage in the material and apply their own knowledge to better understand the study. This research will provide descriptive roles that TNMT plays such as pathway leading to the formation of different substrates including Protoberberine. <ref> Takao, N., Kamigauchi, M., and Okada, M. (1983) Biosynthesis of benzo-[c]phenanthridine alkaloids sanguinarine, chelirubine and macarpine.Helv. Chim. Acta 66, 473–484 CrossRef </ref>
= Structural Highlights =
This protein has a <scene name='82/829888/Catalytic_triad/7'>catalytic triad</scene> which consists of amino acids His-208, Glu-204, and Glu-207. The authors explained within the paper that other amino acids may play a role in the triad as well. They were unsure but those three were the most accurate. These amino acids play an important role in catalysis for the protein. <ref> Bennett, M. R., Thompson, M. L., Shepherd, S. A., Dunstan, M. S., Herbert, A. J., Smith, D. R. M., Cronin, V. A., Menon, B. R. K., Levy, C., and Micklefield, J. (2018) Structure and biocatalytic scope of coclaurine Nmethyltransferase.Angew. Chem. Int. Ed. Engl. 57, 10600–10604CrossRef
Medline </ref>. The basic <scene name='82/829888/Spacefill_view_of_protein/1'>spacefill view</scene> of the entire protein alllows readers to visualize the different elements show in different colors. The elements shown are carbons(grey), nitrogen(blue), and oxygen(red). This protein has a <scene name='82/829888/Ligand/1'>ligand</scene> which is SAM. There are <scene name='82/829888/Hydrophilic_side_chains/1'>hydrophilic side chains</scene> of SAM that form a small catalytic pocket and surrounds the amino group and methyl donor of SAM. This catalytic pocket forms a L shape. In green Glu-204, yellow is Glu-207, red is His-208, and Tyr-81 is blue. There are <scene name='82/823091/Hydrophobic_side_chains/1'>hydrophobic side chains</scene> that consist of Ile-234(purple), Phe-243(green), Phe-257(yellow), Val-262(blue), Met-290(red),and Phe-340(baby blue) which form a isoquinoline pocket. The <scene name='82/829888/Active_site/3'>active site</scene> of the protein consists of amino acids Valine-188(yellow), Aspartic Acid-187(blue), and Alanine-186(green), with purple being the rest of the ligand, SAM. The active site is the region where substrate molecules bind and undergo a chemical reaction. The <scene name='82/829888/Secondary_structure/1'>secondary structure</scene> of this protein contains a pattern of hydrogen bonds between atoms in the peptide bond. This cartoon view allows readers to visualize the alpha(pink) and beta sheets(yellow). The protein consists of two regions which are <scene name='82/829888/Polar_and_non-polar/1'>polar and non-polar regions</scene>. The non-polar region is in grey while the polar region is in purple. The <scene name='82/829888/Cationic_region/1'>cationic region</scene> of the protein has a side chain of Lysine, Arginine, Aspartic Acid, and Glutamic Acid. The cationic region is in the light blue.

= Energy Transformation =
The exact values for kinetic parameters are challenging to determine because of the presence of high levels of apparent substrate and product inhibition. <ref> Liscombe, D. K., Ziegler, J., Schmidt, J., Ammer, C., and Facchini, P.J.
(2009) Targeted metabolite and transcript profiling for elucidating enzyme function: isolation of novel N-methyltransferases from three benzylisoquinoli </ref>
</StructureSection>
== References ==
<references/>

Sandbox Reserved 1567

2019-12-09T01:21:48Z

Deja Sanders:

==Tetrahydroprotoberbine N-methyltransferase==
= Structure =
<StructureSection load='6P3N' size='340' side='right' caption='Tetrahydroprotoberbine' scene=''>
'''Tetrahydroprotoberbine N-methyltransferase''' is a protein thats dimer interface includes six salt 6 salt bridges and 8 hydrogens bonds. It is expressed in E. ''coli'' and crystallized at a pH of 7.0. The crystals were grown in the presence of SAH,SAM, and SAH+SMS. The most significant substrate is SAM which is shown to the right.

= Function =
The protein being studied, Tetrahydroprotoberbine N-methyltransferase, is found in yellow horned poppy (''Glaucium Flavum''). The function of the protein is substate recognition as well as catalysis for the ration engineering of enyzmes for chemoenzymatic synthesis and metabolic engineering. The relative activity of about 8 substrates were tested wiht Protoberberine having the highest percentage. GfTNMT's activity depends on temperature and pH. When the enzyme's activity was at a pH of 8, dropped 10% in activity. 10% activity was also dropped when the temperature was at 30 degrees Celsius. When at 4 degrees Celsius, the activity dropped even more down to 40%. <ref>Liscombe, D. K., and Facchini, P. J. (2007) Molecular cloning and characterization of tetrahydroprotoberberine cis-N-methyltransferase, an enzyme involved in alkaloid biosynthesis in opium poppy. J. Biol. Chem. 282,14741–14751 CrossRef Medline</ref>
= Mutants =
In TMNT, three amino acid residues in the alpha14-helix form one side of the <scene name='82/829888/Binding_pocket/1'>binding pocket</scene> defining the BP region. The binding pocket consists of His-328(green), Ile-329(purple), and Phe-332(orange). The H328 mutation decreases in activity with stylopine and scoulerine producing a 5- and 2-fold while the activity with THP increases 2-fold.
= Relevance =
Studying Tetrahydroprotoberbine will provide commercial application where one will gain a lot of knowledge from both the research paper and online sources. Studying this protein will allow readers to engage in the material and apply their own knowledge to better understand the study. This research will provide descriptive roles that TNMT plays such as pathway leading to the formation of different substrates including Protoberberine. <ref> Takao, N., Kamigauchi, M., and Okada, M. (1983) Biosynthesis of benzo-[c]phenanthridine alkaloids sanguinarine, chelirubine and macarpine.Helv. Chim. Acta 66, 473–484 CrossRef </ref>
= Structural Highlights =
This protein has a <scene name='82/829888/Catalytic_triad/7'>catalytic triad</scene> which consists of amino acids His-208, Glu-204, and Glu-207. The authors explained within the paper that other amino acids may play a role in the triad as well. They were unsure but those three were the most accurate. These amino acids play an important role in catalysis for the protein. <ref> Bennett, M. R., Thompson, M. L., Shepherd, S. A., Dunstan, M. S., Herbert, A. J., Smith, D. R. M., Cronin, V. A., Menon, B. R. K., Levy, C., and Micklefield, J. (2018) Structure and biocatalytic scope of coclaurine Nmethyltransferase.Angew. Chem. Int. Ed. Engl. 57, 10600–10604CrossRef
Medline </ref>. The basic <scene name='82/829888/Spacefill_view_of_protein/1'>spacefill view</scene> of the entire protein alllows readers to visualize the different elements show in different colors. The elements shown are carbons(grey), nitrogen(blue), and oxygen(red). This protein has a <scene name='82/829888/Ligand/1'>ligand</scene> which is SAM. There are <scene name='82/829888/Hydrophilic_side_chains/1'>hydrophilic side chains</scene> of SAM that form a small catalytic pocket and surrounds the amino group and methyl donor of SAM. This catalytic pocket forms a L shape. In green Glu-204, yellow is Glu-207, red is His-208, and Tyr-81 is blue. There are <scene name='82/823091/Hydrophobic_side_chains/1'>hydrophobic side chains</scene> that consist of Ile-234(purple), Phe-243(green), Phe-257(yellow), Val-262(blue), Met-290(red),and Phe-340(baby blue) which form a isoquinoline pocket. The <scene name='82/829888/Active_site/3'>active site</scene> of the protein consists of amino acids Valine-188(yellow), Aspartic Acid-187(blue), and Alanine-186(green), with purple being the rest of the ligand, SAM. The active site is the region where substrate molecules bind and undergo a chemical reaction. The <scene name='82/829888/Secondary_structure/1'>secondary structure</scene> of this protein contains a pattern of hydrogen bonds between atoms in the peptide bond. This cartoon view allows readers to visualize the alpha(pink) and beta sheets(yellow). The protein consists of two regions which are <scene name='82/829888/Polar_and_non-polar/1'>polar and non-polar regions</scene>. The non-polar region is in grey while the polar region is in purple. The <scene name='82/829888/Cationic_region/1'>cationic region</scene> of the protein has a side chain of Lysine, Arginine, Aspartic Acid, and Glutamic Acid. The cationic region is in the light blue.

= Energy Transformation =
The exact values for kinetic parameters are challenging to determine because of the presence of high levels of apparent substrate and product inhibition.
</StructureSection>
== References ==
<references/>

Sandbox Reserved 1567

2019-12-09T00:46:08Z

Deja Sanders:

==Tetrahydroprotoberbine N-methyltransferase==
= Structure =
<StructureSection load='6P3N' size='340' side='right' caption='Tetrahydroprotoberbine' scene=''>
'''Tetrahydroprotoberbine N-methyltransferase''' is a protein thats dimer interface includes six salt 6 salt bridges and 8 hydrogens bonds. It is expressed in E. ''coli'' and crystallized at a pH of 7.0. The crystals were grown in the presence of SAH,SAM, and SAH+SMS. The most significant substrate is SAM which is shown to the right.

= Function =
The protein being studied, Tetrahydroprotoberbine N-methyltransferase, is found in yellow horned poppy (''Glaucium Flavum''). The function of the protein is substate recognition as well as catalysis for the ration engineering of enyzmes for chemoenzymatic synthesis and metabolic engineering. The relative activity of about 8 substrates were tested wiht Protoberberine having the highest percentage. GfTNMT's activity depends on temperature and pH. When the enzyme's activity was at a pH of 8, dropped 10% in activity. 10% activity was also dropped when the temperature was at 30 degrees Celsius. When at 4 degrees Celsius, the activity dropped even more down to 40%.
= Mutants =
In TMNT, three amino acid residues in the alpha14-helix form one side of the <scene name='82/829888/Binding_pocket/1'>binding pocket</scene> defining the BP region. The binding pocket consists of His-328(green), Ile-329(purple), and Phe-332(orange). The H328 mutation decreases in activity with stylopine and scoulerine producing a 5- and 2-fold while the activity with THP increases 2-fold.
= Relevance =
Studying Tetrahydroprotoberbine will provide commercial application where one will gain a lot of knowledge from both the research paper and online sources. Studying this protein will allow readers to engage in the material and apply their own knowledge to better understand the study. This research will provide descriptive roles that TNMT plays such as pathway leading to the formation of different substrates including Protoberberine. <ref> Takao, N., Kamigauchi, M., and Okada, M. (1983) Biosynthesis of benzo-[c]phenanthridine alkaloids sanguinarine, chelirubine and macarpine.Helv. Chim. Acta 66, 473–484 CrossRef </ref>
= Structural Highlights =
This protein has a <scene name='82/829888/Catalytic_triad/7'>catalytic triad</scene> which consists of amino acids His-208, Glu-204, and Glu-207. The authors explained within the paper that other amino acids may play a role in the triad as well. They were unsure but those three were the most accurate. These amino acids play an important role in catalysis for the protein. <ref> Bennett, M. R., Thompson, M. L., Shepherd, S. A., Dunstan, M. S., Herbert, A. J., Smith, D. R. M., Cronin, V. A., Menon, B. R. K., Levy, C., and Micklefield, J. (2018) Structure and biocatalytic scope of coclaurine Nmethyltransferase.Angew. Chem. Int. Ed. Engl. 57, 10600–10604CrossRef
Medline </ref>. The basic <scene name='82/829888/Spacefill_view_of_protein/1'>spacefill view</scene> of the entire protein alllows readers to visualize the different elements show in different colors. The elements shown are carbons(grey), nitrogen(blue), and oxygen(red). This protein has a <scene name='82/829888/Ligand/1'>ligand</scene> which is SAM. There are <scene name='82/829888/Hydrophilic_side_chains/1'>hydrophilic side chains</scene> of SAM that form a small catalytic pocket and surrounds the amino group and methyl donor of SAM. This catalytic pocket forms a L shape. In green Glu-204, yellow is Glu-207, red is His-208, and Tyr-81 is blue. There are <scene name='82/823091/Hydrophobic_side_chains/1'>hydrophobic side chains</scene> that consist of Ile-234(purple), Phe-243(green), Phe-257(yellow), Val-262(blue), Met-290(red),and Phe-340(baby blue) which form a isoquinoline pocket. The <scene name='82/829888/Active_site/3'>active site</scene> of the protein consists of amino acids Valine-188(yellow), Aspartic Acid-187(blue), and Alanine-186(green), with purple being the rest of the ligand, SAM. The active site is the region where substrate molecules bind and undergo a chemical reaction. The <scene name='82/829888/Secondary_structure/1'>secondary structure</scene> of this protein contains a pattern of hydrogen bonds between atoms in the peptide bond. This cartoon view allows readers to visualize the alpha(pink) and beta sheets(yellow). The protein consists of two regions which are <scene name='82/829888/Polar_and_non-polar/1'>polar and non-polar regions</scene>. The non-polar region is in grey while the polar region is in purple. The <scene name='82/829888/Cationic_region/1'>cationic region</scene> of the protein has a side chain of Lysine, Arginine, Aspartic Acid, and Glutamic Acid. The cationic region is in the light blue.

= Energy Transformation =
The exact values for kinetic parameters are challenging to determine because of the presence of high levels of apparent substrate and product inhibition.
</StructureSection>
== References ==
<references/>

Sandbox Reserved 1567

2019-12-08T21:51:30Z

Deja Sanders:

==Tetrahydroprotoberbine N-methyltransferase==
= Structure =
<StructureSection load='6P3N' size='340' side='right' caption='Tetrahydroprotoberbine' scene=''>
'''Tetrahydroprotoberbine N-methyltransferase''' is a protein thats dimer interface includes six salt 6 salt bridges and 8 hydrogens bonds. It is expressed in E. ''coli'' and crystallized at a pH of 7.0. The crystals were grown in the presence of SAH,SAM, and SAH+SMS. The most significant substrate is SAM which is shown to the right.

= Function =
The protein being studied, Tetrahydroprotoberbine N-methyltransferase, is found in yellow horned poppy (''Glaucium Flavum''). The function of the protein is substate recognition as well as catalysis for the ration engineering of enyzmes for chemoenzymatic synthesis and metabolic engineering. The relative activity of about 8 substrates were tested wiht Protoberberine having the highest percentage. GfTNMT's activity depends on temperature and pH. When the enzyme's activity was at a pH of 8, dropped 10% in activity. 10% activity was also dropped when the temperature was at 30 degrees Celsius. When at 4 degrees Celsius, the activity dropped even more down to 40%.
= Mutants =
In TMNT, three amino acid residues in the alpha14-helix form one side of the <scene name='82/829888/Binding_pocket/1'>binding pocket</scene> defining the BP region. The binding pocket consists of His-328(green), Ile-329(purple), and Phe-332(orange). The H328 mutation decreases in activity with stylopine and scoulerine producing a 5- and 2-fold while the activity with THP increases 2-fold.
= Relevance =
Studying Tetrahydroprotoberbine will provide commercial application where one will gain a lot of knowledge from both the research paper and online sources. Studying this protein will allow readers to engage in the material and apply their own knowledge to better understand the study. This research will provide descriptive roles that TNMT plays such as pathway leading to the formation of different substrates including Protoberberine. <ref> Takao, N., Kamigauchi, M., and Okada, M. (1983) Biosynthesis of benzo-[c]phenanthridine alkaloids sanguinarine, chelirubine and macarpine.Helv. Chim. Acta 66, 473–484 CrossRef </ref>
= Structural Highlights =
This protein has a <scene name='82/829888/Catalytic_triad/7'>catalytic triad</scene> which consists of amino acids His-208, Glu-204, and Glu-207. The authors explained within the paper that other amino acids may play a role in the triad as well. They were unsure but those three were the most accurate. These amino acids play an important role in catalysis for the protein. <ref> Bennett, M. R., Thompson, M. L., Shepherd, S. A., Dunstan, M. S., Herbert, A. J., Smith, D. R. M., Cronin, V. A., Menon, B. R. K., Levy, C., and Micklefield, J. (2018) Structure and biocatalytic scope of coclaurine Nmethyltransferase.Angew. Chem. Int. Ed. Engl. 57, 10600–10604CrossRef
Medline </ref>. The basic <scene name='82/829888/Spacefill_view_of_protein/1'>spacefill view</scene> of the entire protein alllows readers to visualize the different elements show in different colors. The elements shown are carbons(grey), nitrogen(blue), and oxygen(red). This protein has a <scene name='82/829888/Ligand/1'>ligand</scene> which is SAM. There are <scene name='82/829888/Hydrophilic_side_chains/1'>hydrophilic side chains</scene> of SAM that form a small catalytic pocket and surrounds the amino group and methyl donor of SAM. This catalytic pocket forms a L shape. In green Glu-204, yellow is Glu-207, red is His-208, and Tyr-81 is blue. There are <scene name='82/823091/Hydrophobic_side_chains/1'>hydrophobic side chains</scene> that consist of Ile-234(purple), Phe-243(green), Phe-257(yellow), Val-262(blue), Met-290(red),and Phe-340(baby blue) which form a isoquinoline pocket. The <scene name='82/829888/Active_site/3'>active site</scene> of the protein consists of amino acids Valine-188(yellow), Aspartic Acid-187(blue), and Alanine-186(green), with purple being the rest of the ligand, SAM. The active site is the region where substrate molecules bind and undergo a chemical reaction. The <scene name='82/829888/Secondary_structure/1'>secondary structure</scene> of this protein contains a pattern of hydrogen bonds between atoms in the peptide bond. This cartoon view allows readers to visualize the alpha(pink) and beta sheets(yellow). The protein consists of two regions which are <scene name='82/829888/Polar_and_non-polar/1'>polar and non-polar regions</scene>. The non-polar region is in grey while the polar region is in purple. The <scene name='82/829888/Cationic_region/1'>cationic region</scene> of the protein has a side chain of Lysine, Arginine, Aspartic Acid, and Glutamic Acid. The cationic region is in the light blue.

= Energy Transformation =
It is challenging to determine the exact values for kinetic parameters because of the presence of high levels of apparent substrate and product inhibition.
</StructureSection>
== References ==
<references/>

Sandbox Reserved 1567

2019-12-08T21:44:11Z

Deja Sanders:

==Tetrahydroprotoberbine N-methyltransferase==
= Structure =
<StructureSection load='6P3N' size='340' side='right' caption='Tetrahydroprotoberbine' scene=''>
'''Tetrahydroprotoberbine N-methyltransferase''' is a protein thats dimer interface includes six salt 6 salt bridges and 8 hydrogens bonds. It is expressed in E. ''coli'' and crystallized at a pH of 7.0. The crystals were grown in the presence of SAH,SAM, and SAH+SMS. The most significant substrate is SAM which is shown to the right.

= Function =
The protein being studied, Tetrahydroprotoberbine N-methyltransferase, is found in yellow horned poppy (''Glaucium Flavum''). The function of the protein is substate recognition as well as catalysis for the ration engineering of enyzmes for chemoenzymatic synthesis and metabolic engineering. The relative activity of about 8 substrates were tested wiht Protoberberine having the highest percentage. GfTNMT's activity depends on temperature and pH. When the enzyme's activity was at a pH of 8, dropped 10% in activity. 10% activity was also dropped when the temperature was at 30 degrees Celsius. When at 4 degrees Celsius, the activity dropped even more down to 40%.
= Mutants =
In TMNT, three amino acid residues in the alpha14-helix form one side of the <scene name='82/829888/Binding_pocket/1'>binding pocket</scene> defining the BP region. The binding pocket consists of His-328(green), Ile-329(purple), and Phe-332(orange). The H328 mutation decreases in activity with stylopine and scoulerine producing a 5- and 2-fold while the activity with THP increases 2-fold.
= Relevance =
Studying Tetrahydroprotoberbine will provide commercial application where one will gain a lot of knowledge from both the research paper and online sources. Studying this protein will allow readers to engage in the material and apply their own knowledge to better understand the study. This research will provide descriptive roles that TNMT plays such as pathway leading to the formation of different substrates including Protoberberine. <ref> Takao, N., Kamigauchi, M., and Okada, M. (1983) Biosynthesis of benzo-[c]phenanthridine alkaloids sanguinarine, chelirubine and macarpine.Helv. Chim. Acta 66, 473–484 CrossRef </ref>
= Structural Highlights =
This protein has a <scene name='82/829888/Catalytic_triad/7'>catalytic triad</scene> which consists of amino acids His-208, Glu-204, and Glu-207. The authors explained within the paper that other amino acids may play a role in the triad as well. They were unsure but those three were the most accurate. These amino acids play an important role in catalysis for the protein. <ref> Bennett, M. R., Thompson, M. L., Shepherd, S. A., Dunstan, M. S., Herbert, A. J., Smith, D. R. M., Cronin, V. A., Menon, B. R. K., Levy, C., and Micklefield, J. (2018) Structure and biocatalytic scope of coclaurine Nmethyltransferase.Angew. Chem. Int. Ed. Engl. 57, 10600–10604CrossRef
Medline </ref>. The basic <scene name='82/829888/Spacefill_view_of_protein/1'>spacefill view</scene> of the entire protein alllows readers to visualize the different elements show in different colors. The elements shown are carbons(grey), nitrogen(blue), and oxygen(red). This protein has a <scene name='82/829888/Ligand/1'>ligand</scene> which is SAM. There are <scene name='82/829888/Hydrophilic_side_chains/1'>hydrophilic side chains</scene> of SAM that form a small catalytic pocket and surrounds the amino group and methyl donor of SAM. This catalytic pocket forms a L shape. In green Glu-204, yellow is Glu-207, red is His-208, and Tyr-81 is blue. There are <scene name='82/823091/Hydrophobic_side_chains/1'>hydrophobic side chains</scene> that consist of Ile-234(purple), Phe-243(green), Phe-257(yellow), Val-262(blue), Met-290(red),and Phe-340(baby blue) which form a isoquinoline pocket. The <scene name='82/829888/Active_site/3'>active site</scene> of the protein consists of amino acids Valine-188(yellow), Aspartic Acid-187(blue), and Alanine-186(green), with purple being the rest of the ligand, SAM. The active site is the region where substrate molecules bind and undergo a chemical reaction. The <scene name='82/829888/Secondary_structure/1'>secondary structure</scene> of this protein contains a pattern of hydrogen bonds between atoms in the peptide bond. This cartoon view allows readers to visualize the alpha(pink) and beta sheets(yellow). The protein consists of two regions which are <scene name='82/829888/Polar_and_non-polar/1'>polar and non-polar regions</scene>. The non-polar region is in grey while the polar region is in purple. The <scene name='82/829888/Cationic_region/1'>cationic region</scene> of the protein has a side chain of Lysine, Arginine, Aspartic Acid, and Glutamic Acid. The cationic region is in the light blue.

= Energy Transformation =
There isn't any energy transformation data presented in the paper.
</StructureSection>

== References ==
<references/>

Sandbox Reserved 1567

2019-12-08T21:25:42Z

Deja Sanders:

==Tetrahydroprotoberbine N-methyltransferase==
= Structure =
<StructureSection load='6P3N' size='340' side='right' caption='Tetrahydroprotoberbine' scene=''>
'''Tetrahydroprotoberbine N-methyltransferase''' is a protein thats dimer interface includes six salt 6 salt bridges and 8 hydrogens bonds. It is expressed in E. ''coli'' and crystallized at a pH of 7.0. The crystals were grown in the presence of SAH,SAM, and SAH+SMS. The most significant substrate is SAM which is shown to the right.

= Function =
The protein being studied, Tetrahydroprotoberbine N-methyltransferase, is found in yellow horned poppy (''Glaucium Flavum''). The function of the protein is substate recognition as well as catalysis for the ration engineering of enyzmes for chemoenzymatic synthesis and metabolic engineering. The relative activity of about 8 substrates were tested wiht Protoberberine having the highest percentage. GfTNMT's activity depends on temperature and pH. When the enzyme's activity was at a pH of 8, dropped 10% in activity. 10% activity was also dropped when the temperature was at 30 degrees Celsius. When at 4 degrees Celsius, the activity dropped even more down to 40%.
= Mutants =
In TMNT, three amino acid residues in the alpha14-helix form one side of the <scene name='82/829888/Binding_pocket/1'>binding pocket</scene> defining the BP region. The binding pocket consists of His-328(green), Ile-329(purple), and Phe-332(orange). The H328 mutation decreases in activity with stylopine and scoulerine producing a 5- and 2-fold while the activity with THP increases 2-fold.
= Relevance =
Studying Tetrahydroprotoberbine will provide commercial application where one will gain a lot of knowledge from both the research paper and online sources. Studying this protein will allow readers to engage in the material and apply their own knowledge to better understand the study. This research will provide descriptive roles that TNMT plays such as pathway leading to the formation of different substrates including Protoberberine. <ref> Takao, N., Kamigauchi, M., and Okada, M. (1983) Biosynthesis of benzo-[c]phenanthridine alkaloids sanguinarine, chelirubine and macarpine.Helv. Chim. Acta 66, 473–484 CrossRef </ref>
= Structural Highlights =
This protein has a <scene name='82/829888/Catalytic_triad/7'>catalytic triad</scene> which consists of amino acids His-208, Glu-204, and Glu-207. The authors explained within the paper that other amino acids may play a role in the triad as well. They were unsure but those three were the most accurate. These amino acids play an important role in catalysis for the protein. <ref> Bennett, M. R., Thompson, M. L., Shepherd, S. A., Dunstan, M. S., Herbert, A. J., Smith, D. R. M., Cronin, V. A., Menon, B. R. K., Levy, C., and Micklefield, J. (2018) Structure and biocatalytic scope of coclaurine Nmethyltransferase.Angew. Chem. Int. Ed. Engl. 57, 10600–10604CrossRef
Medline </ref>. The basic <scene name='82/829888/Spacefill_view_of_protein/1'>spacefill view</scene> of the entire protein alllows readers to visualize the different elements show in different colors. The elements shown are carbons(grey), nitrogen(blue), and oxygen(red). This protein has a <scene name='82/829888/Ligand/1'>ligand</scene> which is SAM. There are <scene name='82/829888/Hydrophilic_side_chains/1'>hydrophilic side chains</scene>of SAM that form a small catalytic pocket and surrounds the amino group and methyl donor of SAM. This catalytic pocket forms a L shape. In green Glu-204, yellow is Glu-207, red is His-208, and Tyr-81 is blue. The <scene name='82/829888/Active_site/3'>active site</scene> of the protein consists of amino acids Valine-188(yellow), Aspartic Acid-187(blue), and Alanine-186(green), with purple being the rest of the ligand, SAM. The active site is the region where substrate molecules bind and undergo a chemical reaction. The <scene name='82/829888/Secondary_structure/1'>secondary structure</scene> of this protein contains a pattern of hydrogen bonds between atoms in the peptide bond. This cartoon view allows readers to visualize the alpha(pink) and beta sheets(yellow). The protein consists of two regions which are <scene name='82/829888/Polar_and_non-polar/1'>polar and non-polar regions</scene>. The non-polar region is in grey while the polar region is in purple. The <scene name='82/829888/Cationic_region/1'>cationic region</scene> of the protein has a side chain of Lysine, Arginine, Aspartic Acid, and Glutamic Acid. The cationic region is in the light blue.

= Energy Transformation =
There isn't any energy transformation data presented in the paper.
</StructureSection>

== References ==
<references/>

Sandbox Reserved 1567

2019-12-02T14:19:48Z

Deja Sanders:

==Tetrahydroprotoberbine N-methyltransferase==
= Structure =
<StructureSection load='6P3N' size='340' side='right' caption='Tetrahydroprotoberbine' scene=''>
'''Tetrahydroprotoberbine N-methyltransferase''' is a protein thats dimer interface includes six salt 6 salt bridges and 8 hydrogens bonds. It is expressed in E. ''coli'' and crystallized at a pH of 7.0. The crystals were grown in the presence of SAH,SAM, and SAH+SMS. Below are the two different substrates that were in the presence of the crystallized protein. The substrate SAM is shown to the right.
[[Image:6p3o.pdb1-500.jpg]]
[[Image:6p3m.pdb1-500.jpg]]
= Function =
The protein being studied, Tetrahydroprotoberbine N-methyltransferase, is found in yellow horned poppy (''Glaucium Flavum''). The function of the protein is substate recognition as well as catalysis for the ration engineering of enyzmes for chemoenzymatic synthesis and metabolic engineering. The relative activity of about 8 substrates were tested wiht Protoberberine having the highest percentage. GfTNMT's activity depends on temperature and pH. When the enzyme's activity was at a pH of 8, dropped 10% in activity. 10% activity was also dropped when the temperature was at 30 degrees Celsius. When at 4 degrees Celsius, the activity dropped even more down to 40%.
= Mutants =
In TMNT, three amino acid residues in the alpha14-helix form one side of the <scene name='82/829888/Binding_pocket/1'>binding pocket</scene> defining the BP region. The binding pocket consists of His-328(green), Ile-329(purple), and Phe-332(orange). The H328 mutation decreases in activity with stylopine and scoulerine producing a 5- and 2-fold while the activity with THP increases 2-fold.
= Relevance =
Studying Tetrahydroprotoberbine will provide commercial application where one will gain a lot of knowledge from both the research paper and online sources. Studying this protein will allow readers to engage in the material and apply their own knowledge to better understand the study. This research will provide descriptive roles that TNMT plays such as pathway leading to the formation of different substrates including Protoberberine. <ref> Takao, N., Kamigauchi, M., and Okada, M. (1983) Biosynthesis of benzo-[c]phenanthridine alkaloids sanguinarine, chelirubine and macarpine.Helv. Chim. Acta 66, 473–484 CrossRef </ref>
= Structural Highlights =
This protein has a <scene name='82/829888/Catalytic_triad/7'>catalytic triad</scene> which consists of amino acids His-208, Glu-204, and Glu-207. The authors explained within the paper that other amino acids may play a role in the triad as well. They were unsure but those three were the most accurate. These amino acids play an important role in catalysis for the protein. <ref> Bennett, M. R., Thompson, M. L., Shepherd, S. A., Dunstan, M. S., Herbert, A. J., Smith, D. R. M., Cronin, V. A., Menon, B. R. K., Levy, C., and Micklefield, J. (2018) Structure and biocatalytic scope of coclaurine Nmethyltransferase.Angew. Chem. Int. Ed. Engl. 57, 10600–10604CrossRef
Medline </ref>. The basic <scene name='82/829888/Spacefill_view_of_protein/1'>spacefill view</scene> of the entire protein alllows readers to visualize the different elements show in different colors. The elements shown are carbons(grey), nitrogen(blue), and oxygen(red). This protein has a <scene name='82/829888/Ligand/1'>ligand</scene> which is SAM. There are <scene name='82/829888/Hydrophilic_side_chains/1'>hydrophilic side chains</scene>of SAM that form a small catalytic pocket and surrounds the amino group and methyl donor of SAM. This catalytic pocket forms a L shape. In green Glu-204, yellow is Glu-207, red is His-208, and Tyr-81 is blue. The <scene name='82/829888/Active_site/3'>active site</scene> of the protein consists of amino acids Valine-188(yellow), Aspartic Acid-187(blue), and Alanine-186(green), with purple being the rest of the ligand, SAM. The active site is the region where substrate molecules bind and undergo a chemical reaction. The <scene name='82/829888/Secondary_structure/1'>secondary structure</scene> of this protein contains a pattern of hydrogen bonds between atoms in the peptide bond. This cartoon view allows readers to visualize the alpha(pink) and beta sheets(yellow). The protein consists of two regions which are <scene name='82/829888/Polar_and_non-polar/1'>polar and non-polar regions</scene>. The non-polar region is in grey while the polar region is in purple. The <scene name='82/829888/Cationic_region/1'>cationic region</scene> of the protein has a side chain of Lysine, Arginine, Aspartic Acid, and Glutamic Acid. The cationic region is in the light blue.

= Energy Transformation =
There isn't any energy transformation data presented in the paper.
</StructureSection>

== References ==
<references/>

Sandbox Reserved 1567

2019-12-02T14:16:11Z

Deja Sanders:

= Structure =
<StructureSection load='6P3N' size='340' side='right' caption='Tetrahydroprotoberbine' scene=''>
'''Tetrahydroprotoberbine N-methyltransferase''' is a protein thats dimer interface includes six salt 6 salt bridges and 8 hydrogens bonds. It is expressed in E. ''coli'' and crystallized at a pH of 7.0. The crystals were grown in the presence of SAH,SAM, and SAH+SMS. Below are the two different substrates that were in the presence of the crystallized protein. The substrate SAM is shown to the right.
[[Image:6p3o.pdb1-500.jpg]]
[[Image:6p3m.pdb1-500.jpg]]
= Function =
The protein being studied, Tetrahydroprotoberbine N-methyltransferase, is found in yellow horned poppy (''Glaucium Flavum''). The function of the protein is substate recognition as well as catalysis for the ration engineering of enyzmes for chemoenzymatic synthesis and metabolic engineering. The relative activity of about 8 substrates were tested wiht Protoberberine having the highest percentage. GfTNMT's activity depends on temperature and pH. When the enzyme's activity was at a pH of 8, dropped 10% in activity. 10% activity was also dropped when the temperature was at 30 degrees Celsius. When at 4 degrees Celsius, the activity dropped even more down to 40%.
= Mutants =
In TMNT, three amino acid residues in the alpha14-helix form one side of the <scene name='82/829888/Binding_pocket/1'>binding pocket</scene> defining the BP region. The binding pocket consists of His-328(green), Ile-329(purple), and Phe-332(orange). The H328 mutation decreases in activity with stylopine and scoulerine producing a 5- and 2-fold while the activity with THP increases 2-fold.
= Relevance =
Studying Tetrahydroprotoberbine will provide commercial application where one will gain a lot of knowledge from both the research paper and online sources. Studying this protein will allow readers to engage in the material and apply their own knowledge to better understand the study. This research will provide descriptive roles that TNMT plays such as pathway leading to the formation of different substrates including Protoberberine. <ref> Takao, N., Kamigauchi, M., and Okada, M. (1983) Biosynthesis of benzo-[c]phenanthridine alkaloids sanguinarine, chelirubine and macarpine.Helv. Chim. Acta 66, 473–484 CrossRef </ref>
= Structural Highlights =
This protein has a <scene name='82/829888/Catalytic_triad/7'>catalytic triad</scene> which consists of amino acids His-208, Glu-204, and Glu-207. The authors explained within the paper that other amino acids may play a role in the triad as well. They were unsure but those three were the most accurate. These amino acids play an important role in catalysis for the protein. <ref> Bennett, M. R., Thompson, M. L., Shepherd, S. A., Dunstan, M. S., Herbert, A. J., Smith, D. R. M., Cronin, V. A., Menon, B. R. K., Levy, C., and Micklefield, J. (2018) Structure and biocatalytic scope of coclaurine Nmethyltransferase.Angew. Chem. Int. Ed. Engl. 57, 10600–10604CrossRef
Medline </ref>. The basic <scene name='82/829888/Spacefill_view_of_protein/1'>spacefill view</scene> of the entire protein alllows readers to visualize the different elements show in different colors. The elements shown are carbons(grey), nitrogen(blue), and oxygen(red). This protein has a <scene name='82/829888/Ligand/1'>ligand</scene> which is SAM. There are <scene name='82/829888/Hydrophilic_side_chains/1'>hydrophilic side chains</scene>of SAM that form a small catalytic pocket and surrounds the amino group and methyl donor of SAM. This catalytic pocket forms a L shape. In green Glu-204, yellow is Glu-207, red is His-208, and Tyr-81 is blue. The <scene name='82/829888/Active_site/3'>active site</scene> of the protein consists of amino acids Valine-188(yellow), Aspartic Acid-187(blue), and Alanine-186(green), with purple being the rest of the ligand, SAM. The active site is the region where substrate molecules bind and undergo a chemical reaction. The <scene name='82/829888/Secondary_structure/1'>secondary structure</scene> of this protein contains a pattern of hydrogen bonds between atoms in the peptide bond. This cartoon view allows readers to visualize the alpha(pink) and beta sheets(yellow). The protein consists of two regions which are <scene name='82/829888/Polar_and_non-polar/1'>polar and non-polar regions</scene>. The non-polar region is in grey while the polar region is in purple. The <scene name='82/829888/Cationic_region/1'>cationic region</scene> of the protein has a side chain of Lysine, Arginine, Aspartic Acid, and Glutamic Acid. The cationic region is in the light blue.

= Energy Transformation =
There isn't any energy transformation data presented in the paper.
</StructureSection>

== References ==
<references/>

Tetrahydroprotoberberine N-methyltransferase

2019-12-01T04:43:46Z

Deja Sanders:

Tetrahydroprotoberberine N-methyltransferase

2019-12-01T04:36:30Z

Deja Sanders:

= Structure =
<StructureSection load='6P3N' size='340' side='right' caption='Tetrahydroprotoberbine' scene=''>
'''Tetrahydroprotoberbine N-methyltransferase''' is a protein thats dimer interface includes six salt 6 salt bridges and 8 hydrogens bonds. It is expressed in E. ''coli'' and crystallized at a pH of 7.0. The crystals were grown in the presence of SAH,SAM, and SAH+SMS. Below are the two different substrates that were in the presence of the crystallized protein. The substrate SAM is shown to the right.
[[Image:6p3o.pdb1-500.jpg]]
[[Image:6p3m.pdb1-500.jpg]]
= Function =
The protein being studied, Tetrahydroprotoberbine N-methyltransferase, is found in yellow horned poppy (''Glaucium Flavum''). The function of the protein is substate recognition as well as catalysis for the ration engineering of enyzmes for chemoenzymatic synthesis and metabolic engineering. The relative activity of about 8 substrates were tested wiht Protoberberine having the highest percentage. GfTNMT's activity depends on temperature and pH. When the enzyme's activity was at a pH of 8, dropped 10% in activity. 10% activity was also dropped when the temperature was at 30 degrees Celsius. When at 4 degrees Celsius, the activity dropped even more down to 40%.
= Mutants =
In TMNT, three amino acid residues in the alpha14-helix form one side of the <scene name='82/829888/Binding_pocket/1'>binding pocket</scene> defining the BP region. The binding pocket consists of His-328(green), Ile-329(purple), and Phe-332(orange). The H328 mutation decreases in activity with stylopine and scoulerine producing a 5- and 2-fold while the activity with THP increases 2-fold.
= Relevance =
Studying Tetrahydroprotoberbine will provide commercial application where one will gain a lot of knowledge from both the research paper and online sources. Studying this protein will allow readers to engage in the material and apply their own knowledge to better understand the study. This research will provide descriptive roles that TNMT plays such as pathway leading to the formation of different substrates including Protoberberine. <ref> Takao, N., Kamigauchi, M., and Okada, M. (1983) Biosynthesis of benzo-[c]phenanthridine alkaloids sanguinarine, chelirubine and macarpine.Helv. Chim. Acta 66, 473–484 CrossRef </ref>
= Structural Highlights =
This protein has a <scene name='82/829888/Catalytic_triad/7'>catalytic triad</scene> which consists of amino acids His-208, Glu-204, and Glu-207. The authors explained within the paper that other amino acids may play a role in the triad as well. They were unsure but those three were the most accurate. These amino acids play an important role in catalysis for the protein. <ref> Bennett, M. R., Thompson, M. L., Shepherd, S. A., Dunstan, M. S., Herbert, A. J., Smith, D. R. M., Cronin, V. A., Menon, B. R. K., Levy, C., and Micklefield, J. (2018) Structure and biocatalytic scope of coclaurine Nmethyltransferase.Angew. Chem. Int. Ed. Engl. 57, 10600–10604CrossRef
Medline </ref>. The basic <scene name='82/829888/Spacefill_view_of_protein/1'>spacefill view</scene> of the entire protein alllows readers to visualize the different elements show in different colors. The elements shown are carbons(grey), nitrogen(blue), and oxygen(red). This protein has a <scene name='82/829888/Ligand/1'>ligand</scene> which is SAM. There are <scene name='82/829888/Hydrophilic_side_chains/1'>hydrophilic side chains</scene>of SAM that form a small catalytic pocket and surrounds the amino group and methyl donor of SAM. This catalytic pocket forms a L shape. In green Glu-204, yellow is Glu-207, red is His-208, and Tyr-81 is blue. The <scene name='82/829888/Active_site/3'>active site</scene> of the protein consists of amino acids Valine-188(yellow), Aspartic Acid-187(blue), and Alanine-186(green), with purple being the rest of the ligand, SAM. The active site is the region where substrate molecules bind and undergo a chemical reaction. The <scene name='82/829888/Secondary_structure/1'>secondary structure</scene> of this protein contains a pattern of hydrogen bonds between atoms in the peptide bond. This cartoon view allows readers to visualize the alpha(pink) and beta sheets(yellow). The protein consists of two regions which are <scene name='82/829888/Polar_and_non-polar/1'>polar and non-polar regions</scene>. The non-polar region is in grey while the polar region is in purple. The <scene name='82/829888/Cationic_region/1'>cationic region</scene> of the protein has a side chain of Lysine, Arginine, Aspartic Acid, and Glutamic Acid. The cationic region is in the light blue.
</StructureSection>

== References ==
<references/>

Tetrahydroprotoberberine N-methyltransferase

2019-12-01T04:32:24Z

Deja Sanders:

= Structure =
<StructureSection load='6P3N' size='340' side='right' caption='Tetrahydroprotoberbine' scene=''>
'''Tetrahydroprotoberbine N-methyltransferase''' is a protein thats dimer interface includes six salt 6 salt bridges and 8 hydrogens bonds. It is expressed in E. ''coli'' and crystallized at a pH of 7.0. The crystals were grown in the presence of SAH,SAM, and SAH+SMS. Below are the two different substrates that were in the presence of the crystallized protein. The substrate SAM is shown to the right.
[[Image:6p3o.pdb1-500.jpg]]
[[Image:6p3m.pdb1-500.jpg]]
= Function =
The protein being studied, Tetrahydroprotoberbine N-methyltransferase, is found in yellow horned poppy (''Glaucium Flavum''). The function of the protein is substate recognition as well as catalysis for the ration engineering of enyzmes for chemoenzymatic synthesis and metabolic engineering. The relative activity of about 8 substrates were tested wiht Protoberberine having the highest percentage. GfTNMT's activity depends on temperature and pH. When the enzyme's activity was at a pH of 8, dropped 10% in activity. 10% activity was also dropped when the temperature was at 30 degrees Celsius. When at 4 degrees Celsius, the activity dropped even more down to 40%.
= Mutants =
In TMNT, three amino acid residues in the alpha14-helix form one side of the <scene name='82/829888/Binding_pocket/1'>binding pocket</scene> defining the BP region. The binding pocket consists of His-328(green), Ile-329(purple), and Phe-332(orange). The H328 mutation decreases in activity with stylopine and scoulerine producing a 5- and 2-fold while the activity with THP increases 2-fold.
= Relevance =
Studying Tetrahydroprotoberbine will provide commercial application where one will gain a lot of knowledge from both the research paper and online sources. Studying this protein will allow readers to engage in the material and apply their own knowledge to better understand the study. This research will provide descriptive roles that TNMT plays such as pathway leading to the formation of different substrates including Protoberberine. <ref> Takao, N., Kamigauchi, M., and Okada, M. (1983) Biosynthesis of benzo-[c]phenanthridine alkaloids sanguinarine, chelirubine and macarpine.Helv. Chim. Acta 66, 473–484 CrossRef </ref>
= Structural Highlights =
This protein has a <scene name='82/829888/Catalytic_triad/7'>catalytic triad</scene> which consists of amino acids His-208, Glu-204, and Glu-207. The authors explained within the paper that other amino acids may play a role in the triad as well. They were unsure but those three were the most accurate. These amino acids play an important role in catalysis for the protein. <ref> 20069275 </ref> The basic <scene name='82/829888/Spacefill_view_of_protein/1'>spacefill view</scene> of the entire protein alllows readers to visualize the different elements show in different colors. The elements shown are carbons(grey), nitrogen(blue), and oxygen(red). This protein has a <scene name='82/829888/Ligand/1'>ligand</scene> which is SAM. There are <scene name='82/829888/Hydrophilic_side_chains/1'>hydrophilic side chains</scene>of SAM that form a small catalytic pocket and surrounds the amino group and methyl donor of SAM. This catalytic pocket forms a L shape. In green Glu-204, yellow is Glu-207, red is His-208, and Tyr-81 is blue. The <scene name='82/829888/Active_site/3'>active site</scene> of the protein consists of amino acids Valine-188(yellow), Aspartic Acid-187(blue), and Alanine-186(green), with purple being the rest of the ligand, SAM. The active site is the region where substrate molecules bind and undergo a chemical reaction. The <scene name='82/829888/Secondary_structure/1'>secondary structure</scene> of this protein contains a pattern of hydrogen bonds between atoms in the peptide bond. This cartoon view allows readers to visualize the alpha(pink) and beta sheets(yellow). The protein consists of two regions which are <scene name='82/829888/Polar_and_non-polar/1'>polar and non-polar regions</scene>. The non-polar region is in grey while the polar region is in purple. The <scene name='82/829888/Cationic_region/1'>cationic region</scene> of the protein has a side chain of Lysine, Arginine, Aspartic Acid, and Glutamic Acid. The cationic region is in the light blue.
</StructureSection>

== References ==
<references/>

Tetrahydroprotoberberine N-methyltransferase

2019-12-01T04:15:40Z

Deja Sanders:

= Structure =
<StructureSection load='6P3N' size='340' side='right' caption='Tetrahydroprotoberbine' scene=''>
'''Tetrahydroprotoberbine N-methyltransferase''' is a protein thats dimer interface includes six salt 6 salt bridges and 8 hydrogens bonds. It is expressed in E. ''coli'' and crystallized at a pH of 7.0. The crystals were grown in the presence of SAH,SAM, and SAH+SMS. Below are the two different substrates that were in the presence of the crystallized protein. The substrate SAM is shown to the right.
[[Image:6p3o.pdb1-500.jpg]]
[[Image:6p3m.pdb1-500.jpg]]
= Function =
The protein being studied, Tetrahydroprotoberbine N-methyltransferase, is found in yellow horned poppy (''Glaucium Flavum''). The function of the protein is substate recognition as well as catalysis for the ration engineering of enyzmes for chemoenzymatic synthesis and metabolic engineering. The relative activity of about 8 substrates were tested wiht Protoberberine having the highest percentage. GfTNMT's activity depends on temperature and pH. When the enzyme's activity was at a pH of 8, dropped 10% in activity. 10% activity was also dropped when the temperature was at 30 degrees Celsius. When at 4 degrees Celsius, the activity dropped even more down to 40%.
= Mutants =
In TMNT, three amino acid residues in the alpha14-helix form one side of the <scene name='82/829888/Binding_pocket/1'>binding pocket</scene> defining the BP region. The binding pocket consists of His-328(green), Ile-329(purple), and Phe-332(orange). The H328 mutation decreases in activity with stylopine and scoulerine producing a 5- and 2-fold while the activity with THP increases 2-fold.
= Relevance =
Studying Tetrahydroprotoberbine will provide commercial application where one will gain a lot of knowledge from both the research paper and online sources. Studying this protein will allow readers to engage in the material and apply their own knowledge to better understand the study. This research will provide descriptive roles that TNMT plays such as pathway leading to the formation of different substrates including Protoberberine. <ref> 31395658 </ref>
= Structural Highlights =
This protein has a <scene name='82/829888/Catalytic_triad/7'>catalytic triad</scene> which consists of amino acids His-208, Glu-204, and Glu-207. The authors explained within the paper that other amino acids may play a role in the triad as well. They were unsure but those three were the most accurate. These amino acids play an important role in catalysis for the protein. <ref> 20069275 </ref> The basic <scene name='82/829888/Spacefill_view_of_protein/1'>spacefill view</scene> of the entire protein alllows readers to visualize the different elements show in different colors. The elements shown are carbons(grey), nitrogen(blue), and oxygen(red). This protein has a <scene name='82/829888/Ligand/1'>ligand</scene> which is SAM. There are <scene name='82/829888/Hydrophilic_side_chains/1'>hydrophilic side chains</scene>of SAM that form a small catalytic pocket and surrounds the amino group and methyl donor of SAM. This catalytic pocket forms a L shape. In green Glu-204, yellow is Glu-207, red is His-208, and Tyr-81 is blue. The <scene name='82/829888/Active_site/3'>active site</scene> of the protein consists of amino acids Valine-188(yellow), Aspartic Acid-187(blue), and Alanine-186(green), with purple being the rest of the ligand, SAM. The active site is the region where substrate molecules bind and undergo a chemical reaction. The <scene name='82/829888/Secondary_structure/1'>secondary structure</scene> of this protein contains a pattern of hydrogen bonds between atoms in the peptide bond. This cartoon view allows readers to visualize the alpha(pink) and beta sheets(yellow). The protein consists of two regions which are <scene name='82/829888/Polar_and_non-polar/1'>polar and non-polar regions</scene>. The non-polar region is in grey while the polar region is in purple. The <scene name='82/829888/Cationic_region/1'>cationic region</scene> of the protein has a side chain of Lysine, Arginine, Aspartic Acid, and Glutamic Acid. The cationic region is in the light blue.
</StructureSection>

== References ==

Tetrahydroprotoberberine N-methyltransferase

2019-11-30T16:19:31Z

Deja Sanders:

= Structure =
<StructureSection load='6P3N' size='340' side='right' caption='Tetrahydroprotoberbine' scene=''>
'''Tetrahydroprotoberbine N-methyltransferase''' is a protein thats dimer interface includes six salt 6 salt bridges and 8 hydrogens bonds. It is expressed in E. ''coli'' and crystallized at a pH of 7.0. The crystals were grown in the presence of SAH,SAM, and SAH+SMS. Below are the two different substrates that were in the presence of the crystallized protein. The substrate SAM is shown to the right.
[[Image:6p3o.pdb1-500.jpg]]
[[Image:6p3m.pdb1-500.jpg]]
= Function =
The protein being studied, Tetrahydroprotoberbine N-methyltransferase, is found in yellow horned poppy (''Glaucium Flavum''). The function of the protein is substate recognition as well as catalysis for the ration engineering of enyzmes for chemoenzymatic synthesis and metabolic engineering. The relative activity of about 8 substrates were tested wiht Protoberberine having the highest percentage. GfTNMT's activity depends on temperature and pH. When the enzyme's activity was at a pH of 8, dropped 10% in activity. 10% activity was also dropped when the temperature was at 30 degrees Celsius. When at 4 degrees Celsius, the activity dropped even more down to 40%.
= Mutants =
In TMNT, three amino acid residues in the alpha14-helix form one side of the <scene name='82/829888/Binding_pocket/1'>binding pocket</scene> defining the BP region. The binding pocket consists of His-328(green), Ile-329(purple), and Phe-332(orange). The H328 mutation decreases in activity with stylopine and scoulerine producing a 5- and 2-fold while the activity with THP increases 2-fold.
= Relevance =
Studying Tetrahydroprotoberbine will provide commercial application where one will gain a lot of knowledge from both the research paper and online sources. Studying this protein will allow readers to engage in the material and apply their own knowledge to better understand the study. This research will provide descriptive roles that TNMT plays such as pathway leading to the formation of different substrates including Protoberberine. <ref>20069275 </ref>
= Structural Highlights =
This protein has a <scene name='82/829888/Catalytic_triad/7'>catalytic triad</scene> which consists of amino acids His-208, Glu-204, and Glu-207. The authors explained within the paper that other amino acids may play a role in the triad as well. They were unsure but those three were the most accurate. These amino acids play an important role in catalysis for the protein. <ref> 20069275 </ref> The basic <scene name='82/829888/Spacefill_view_of_protein/1'>spacefill view</scene> of the entire protein alllows readers to visualize the different elements show in different colors. The elements shown are carbons(grey), nitrogen(blue), and oxygen(red). This protein has a <scene name='82/829888/Ligand/1'>ligand</scene> which is SAM. There are <scene name='82/829888/Hydrophilic_side_chains/1'>hydrophilic side chains</scene>of SAM that form a small catalytic pocket and surrounds the amino group and methyl donor of SAM. This catalytic pocket forms a L shape. In green Glu-204, yellow is Glu-207, red is His-208, and Tyr-81 is blue. The <scene name='82/829888/Active_site/3'>active site</scene> of the protein consists of amino acids Valine-188(yellow), Aspartic Acid-187(blue), and Alanine-186(green), with purple being the rest of the ligand, SAM. The active site is the region where substrate molecules bind and undergo a chemical reaction. The <scene name='82/829888/Secondary_structure/1'>secondary structure</scene> of this protein contains a pattern of hydrogen bonds between atoms in the peptide bond. This cartoon view allows readers to visualize the alpha(pink) and beta sheets(yellow). The protein consists of two regions which are <scene name='82/829888/Polar_and_non-polar/1'>polar and non-polar regions</scene>. The non-polar region is in grey while the polar region is in purple. The <scene name='82/829888/Cationic_region/1'>cationic region</scene> of the protein has a side chain of Lysine, Arginine, Aspartic Acid, and Glutamic Acid. The cationic region is in the light blue.
</StructureSection>

== References ==

Tetrahydroprotoberberine N-methyltransferase

2019-11-30T16:14:15Z

Deja Sanders:

= Structure =
<StructureSection load='6P3N' size='340' side='right' caption='Tetrahydroprotoberbine' scene=''>
'''Tetrahydroprotoberbine N-methyltransferase''' is a protein thats dimer interface includes six salt 6 salt bridges and 8 hydrogens bonds. It is expressed in E. ''coli'' and crystallized at a pH of 7.0. The crystals were grown in the presence of SAH,SAM, and SAH+SMS. Below are the two different substrates that were in the presence of the crystallized protein. The substrate SAM is shown to the right.
[[Image:6p3o.pdb1-500.jpg]]
[[Image:6p3m.pdb1-500.jpg]]
= Function =
The protein being studied, Tetrahydroprotoberbine N-methyltransferase, is found in yellow horned poppy (''Glaucium Flavum''). The function of the protein is substate recognition as well as catalysis for the ration engineering of enyzmes for chemoenzymatic synthesis and metabolic engineering. The relative activity of about 8 substrates were tested wiht Protoberberine having the highest percentage. GfTNMT's activity depends on temperature and pH. When the enzyme's activity was at a pH of 8, dropped 10% in activity. 10% activity was also dropped when the temperature was at 30 degrees Celsius. When at 4 degrees Celsius, the activity dropped even more down to 40%.
= Mutants =
In TMNT, three amino acid residues in the alpha14-helix form one side of the <scene name='82/829888/Binding_pocket/1'>binding pocket</scene> defining the BP region. The binding pocket consists of His-328(green), Ile-329(purple), and Phe-332(orange). The H328 mutation decreases in activity with stylopine and scoulerine producing a 5- and 2-fold while the activity with THP increases 2-fold.
= Relevance =
Studying Tetrahydroprotoberbine will provide commercial application where one will gain a lot of knowledge from both the research paper and online sources. Studying this protein will allow readers to engage in the material and apply their own knowledge to better understand the study. This research will provide descriptive roles that TNMT plays such as pathway leading to the formation of different substrates including Protoberberine. <ref>20069275 </ref>
= Structural Highlights =
This protein has a <scene name='82/829888/Catalytic_triad/7'>catalytic triad</scene> which consists of amino acids His-208, Glu-204, and Glu-207. The authors explained within the paper that other amino acids may play a role in the triad as well. They were unsure but those three were the most accurate. These amino acids play an important role in catalysis for the protein. <ref> 20069275 </ref> The basic <scene name='82/829888/Spacefill_view_of_protein/1'>spacefill view</scene> of the entire protein alllows readers to visualize the different elements show in different colors. The elements shown are carbons(grey), nitrogen(blue), and oxygen(red). This protein has a <scene name='82/829888/Ligand/1'>ligand</scene> which is SAM. There are <scene name='82/829888/Hydrophilic_side_chains/1'>hydrophilic side chains</scene>of SAM that form a small catalytic pocket and surrounds the amino group and methyl donor of SAM. This catalytic pocket forms a L shape. In green Glu-204, yellow is Glu-207, red is His-208, and Tyr-81 is blue. The <scene name='82/829888/Active_site/3'>active site</scene> of the protein consists of amino acids Valine-188(yellow), Aspartic Acid-187(blue), and Alanine-186(green), with purple being the rest of the ligand, SAM. The active site is the region where substrate molecules bind and undergo a chemical reaction. The <scene name='82/829888/Secondary_structure/1'>secondary structure</scene> of this protein contains a pattern of hydrogen bonds between atoms in the peptide bond. This cartoon view allows readers to visualize the alpha(pink) and beta sheets(yellow). The protein consists of two regions which are <scene name='82/829888/Polar_and_non-polar/1'>polar and non-polar regions</scene>. The non-polar region is in grey while the polar region is in purple.
</StructureSection>

== References ==

Tetrahydroprotoberberine N-methyltransferase

2019-11-30T16:00:14Z

Deja Sanders:

= Structure =
<StructureSection load='6P3N' size='340' side='right' caption='Tetrahydroprotoberbine' scene=''>
'''Tetrahydroprotoberbine N-methyltransferase''' is a protein thats dimer interface includes six salt 6 salt bridges and 8 hydrogens bonds. It is expressed in E. ''coli'' and crystallized at a pH of 7.0. The crystals were grown in the presence of SAH,SAM, and SAH+SMS. Below are the two different substrates that were in the presence of the crystallized protein. The substrate SAM is shown to the right.
[[Image:6p3o.pdb1-500.jpg]]
[[Image:6p3m.pdb1-500.jpg]]
= Function =
The protein being studied, Tetrahydroprotoberbine N-methyltransferase, is found in yellow horned poppy (''Glaucium Flavum''). The function of the protein is substate recognition as well as catalysis for the ration engineering of enyzmes for chemoenzymatic synthesis and metabolic engineering. The relative activity of about 8 substrates were tested wiht Protoberberine having the highest percentage. GfTNMT's activity depends on temperature and pH. When the enzyme's activity was at a pH of 8, dropped 10% in activity. 10% activity was also dropped when the temperature was at 30 degrees Celsius. When at 4 degrees Celsius, the activity dropped even more down to 40%.
= Mutants =
In TMNT, three amino acid residues in the alpha14-helix form one side of the <scene name='82/829888/Binding_pocket/1'>binding pocket</scene> defining the BP region. The binding pocket consists of His-328(green), Ile-329(purple), and Phe-332(orange). The H328 mutation decreases in activity with stylopine and scoulerine producing a 5- and 2-fold while the activity with THP increases 2-fold.
= Relevance =
Studying Tetrahydroprotoberbine will provide commercial application where one will gain a lot of knowledge from both the research paper and online sources. Studying this protein will allow readers to engage in the material and apply their own knowledge to better understand the study. This research will provide descriptive roles that TNMT plays such as pathway leading to the formation of different substrates including Protoberberine. <ref>20069275 </ref>
= Structural Highlights =
This protein has a <scene name='82/829888/Catalytic_triad/7'>catalytic triad</scene> which consists of amino acids His-208, Glu-204, and Glu-207. The authors explained within the paper that other amino acids may play a role in the triad as well. They were unsure but those three were the most accurate. These amino acids play an important role in catalysis for the protein. <ref> 20069275 </ref> The basic <scene name='82/829888/Spacefill_view_of_protein/1'>spacefill view</scene> of the entire protein alllows readers to visualize the different elements show in different colors. The elements shown are carbons(grey), nitrogen(blue), and oxygen(red). This protein has a <scene name='82/829888/Ligand/1'>ligand</scene> which is SAM. There are <scene name='82/829888/Hydrophilic_side_chains/1'>hydrophilic side chains</scene>of SAM that form a small catalytic pocket and surrounds the amino group and methyl donor of SAM. This catalytic pocket forms a L shape. In green Glu-204, yellow is Glu-207, red is His-208, and Tyr-81 is blue. The <scene name='82/829888/Active_site/3'>active site</scene> of the protein consists of amino acids Valine-188(yellow), Aspartic Acid-187(blue), and Alanine-186(green), with purple being the rest of the ligand, SAM. The active site is the region where substrate molecules bind and undergo a chemical reaction. The <scene name='82/829888/Secondary_structure/1'>secondary structure</scene> of this protein contains a pattern of hydrogen bonds between atoms in the peptide bond. This cartoon view allows readers to visualize the alpha(pink) and beta sheets(yellow).
</StructureSection>

== References ==

Tetrahydroprotoberberine N-methyltransferase

2019-11-30T15:53:05Z

Deja Sanders:

= Structure =
<StructureSection load='6P3N' size='340' side='right' caption='Tetrahydroprotoberbine' scene=''>
'''Tetrahydroprotoberbine N-methyltransferase''' is a protein thats dimer interface includes six salt 6 salt bridges and 8 hydrogens bonds. It is expressed in E. ''coli'' and crystallized at a pH of 7.0. The crystals were grown in the presence of SAH,SAM, and SAH+SMS. Below are the two different substrates that were in the presence of the crystallized protein. The substrate SAM is shown to the right.
[[Image:6p3o.pdb1-500.jpg]]
[[Image:6p3m.pdb1-500.jpg]]
= Function =
The protein being studied, Tetrahydroprotoberbine N-methyltransferase, is found in yellow horned poppy (''Glaucium Flavum''). The function of the protein is substate recognition as well as catalysis for the ration engineering of enyzmes for chemoenzymatic synthesis and metabolic engineering. The relative activity of about 8 substrates were tested wiht Protoberberine having the highest percentage. GfTNMT's activity depends on temperature and pH. When the enzyme's activity was at a pH of 8, dropped 10% in activity. 10% activity was also dropped when the temperature was at 30 degrees Celsius. When at 4 degrees Celsius, the activity dropped even more down to 40%.
= Mutants =
In TMNT, three amino acid residues in the alpha14-helix form one side of the <scene name='82/829888/Binding_pocket/1'>binding pocket</scene> defining the BP region. The binding pocket consists of His-328(green), Ile-329(purple), and Phe-332(orange). The H328 mutation decreases in activity with stylopine and scoulerine producing a 5- and 2-fold while the activity with THP increases 2-fold.
= Relevance =
Studying Tetrahydroprotoberbine will provide commercial application where one will gain a lot of knowledge from both the research paper and online sources. Studying this protein will allow readers to engage in the material and apply their own knowledge to better understand the study. This research will provide descriptive roles that TNMT plays such as pathway leading to the formation of different substrates including Protoberberine. <ref>20069275 </ref>
= Structural Highlights =
This protein has a <scene name='82/829888/Catalytic_triad/7'>catalytic triad</scene> which consists of amino acids His-208, Glu-204, and Glu-207. The authors explained within the paper that other amino acids may play a role in the triad as well. They were unsure but those three were the most accurate. These amino acids play an important role in catalysis for the protein. <ref> 20069275 </ref> The basic <scene name='82/829888/Spacefill_view_of_protein/1'>spacefill view</scene> of the entire protein alllows readers to visualize the different elements show in different colors. The elements shown are carbons(grey), nitrogen(blue), and oxygen(red). This protein has a <scene name='82/829888/Ligand/1'>ligand</scene> which is SAM. There are <scene name='82/829888/Hydrophilic_side_chains/1'>hydrophilic side chains</scene>of SAM that form a small catalytic pocket and surrounds the amino group and methyl donor of SAM. This catalytic pocket forms a L shape. In green Glu-204, yellow is Glu-207, red is His-208, and Tyr-81 is blue. The <scene name='82/829888/Active_site/3'>active site</scene> of the protein consists of amino acids Valine-188(yellow), Aspartic Acid-187(blue), and Alanine-186(green), with purple being the rest of the ligand, SAM. The active site is the region where substrate molecules bind and undergo a chemical reaction.
</StructureSection>

== References ==

Tetrahydroprotoberberine N-methyltransferase

2019-11-30T15:51:43Z

Deja Sanders:

= Structure =
<StructureSection load='6P3N' size='340' side='right' caption='Tetrahydroprotoberbine' scene=''>
'''Tetrahydroprotoberbine N-methyltransferase''' is a protein thats dimer interface includes six salt 6 salt bridges and 8 hydrogens bonds. It is expressed in E. ''coli'' and crystallized at a pH of 7.0. The crystals were grown in the presence of SAH,SAM, and SAH+SMS. Below are the two different substrates that were in the presence of the crystallized protein. The substrate SAM is shown to the right.
[[Image:6p3o.pdb1-500.jpg]]
[[Image:6p3m.pdb1-500.jpg]]
= Function =
The protein being studied, Tetrahydroprotoberbine N-methyltransferase, is found in yellow horned poppy (''Glaucium Flavum''). The function of the protein is substate recognition as well as catalysis for the ration engineering of enyzmes for chemoenzymatic synthesis and metabolic engineering. The relative activity of about 8 substrates were tested wiht Protoberberine having the highest percentage. GfTNMT's activity depends on temperature and pH. When the enzyme's activity was at a pH of 8, dropped 10% in activity. 10% activity was also dropped when the temperature was at 30 degrees Celsius. When at 4 degrees Celsius, the activity dropped even more down to 40%.
= Mutants =
In TMNT, three amino acid residues in the alpha14-helix form one side of the <scene name='82/829888/Binding_pocket/1'>binding pocket</scene> defining the BP region. The binding pocket consists of His-328(green), Ile-329(purple), and Phe-332(orange). The H328 mutation decreases in activity with stylopine and scoulerine producing a 5- and 2-fold while the activity with THP increases 2-fold.
= Relevance =
Studying Tetrahydroprotoberbine will provide commercial application where one will gain a lot of knowledge from both the research paper and online sources. Studying this protein will allow readers to engage in the material and apply their own knowledge to better understand the study. This research will provide descriptive roles that TNMT plays such as pathway leading to the formation of different substrates including Protoberberine. <ref>20069275 </ref>
= Structural Highlights =
This protein has a <scene name='82/829888/Catalytic_triad/7'>catalytic triad</scene> which consists of amino acids His-208, Glu-204, and Glu-207. The authors explained within the paper that other amino acids may play a role in the triad as well. They were unsure but those three were the most accurate. These amino acids play an important role in catalysis for the protein. <ref> 20069275 </ref> The basic <scene name='82/829888/Spacefill_view_of_protein/1'>spacefill view</scene> of the entire protein alllows readers to visualize the different elements show in different colors. The elements shown are carbons(grey), nitrogen(blue), and oxygen(red). This protein has a <scene name='82/829888/Ligand/1'>Ligand</scene> which is SAM. There are <scene name='82/829888/Hydrophilic_side_chains/1'>hydrophilic side chains</scene>of SAM that form a small catalytic pocket and surrounds the amino group and methyl donor of SAM. This catalytic pocket forms a L shape. In green Glu-204, yellow is Glu-207, red is His-208, and Tyr-81 is blue. The <scene name='82/829888/Active_site/3'>active site</scene> of the protein consists of amino acids Valine-188(yellow), Aspartic Acid-187(blue), and Alanine-186(green), with purple being the rest of the ligand, SAM.
</StructureSection>

== References ==

Tetrahydroprotoberberine N-methyltransferase

2019-11-30T15:46:41Z

Deja Sanders:

= Structure =
<StructureSection load='6P3N' size='340' side='right' caption='Tetrahydroprotoberbine' scene=''>
'''Tetrahydroprotoberbine N-methyltransferase''' is a protein thats dimer interface includes six salt 6 salt bridges and 8 hydrogens bonds. It is expressed in E. ''coli'' and crystallized at a pH of 7.0. The crystals were grown in the presence of SAH,SAM, and SAH+SMS. Below are the two different substrates that were in the presence of the crystallized protein. The substrate SAM is shown to the right.
[[Image:6p3o.pdb1-500.jpg]]
[[Image:6p3m.pdb1-500.jpg]]
= Function =
The protein being studied, Tetrahydroprotoberbine N-methyltransferase, is found in yellow horned poppy (''Glaucium Flavum''). The function of the protein is substate recognition as well as catalysis for the ration engineering of enyzmes for chemoenzymatic synthesis and metabolic engineering. The relative activity of about 8 substrates were tested wiht Protoberberine having the highest percentage. GfTNMT's activity depends on temperature and pH. When the enzyme's activity was at a pH of 8, dropped 10% in activity. 10% activity was also dropped when the temperature was at 30 degrees Celsius. When at 4 degrees Celsius, the activity dropped even more down to 40%.
= Mutants =
In TMNT, three amino acid residues in the alpha14-helix form one side of the <scene name='82/829888/Binding_pocket/1'>binding pocket</scene> defining the BP region. The binding pocket consists of His-328(green), Ile-329(purple), and Phe-332(orange). The H328 mutation decreases in activity with stylopine and scoulerine producing a 5- and 2-fold while the activity with THP increases 2-fold.
= Relevance =
Studying Tetrahydroprotoberbine will provide commercial application where one will gain a lot of knowledge from both the research paper and online sources. Studying this protein will allow readers to engage in the material and apply their own knowledge to better understand the study. This research will provide descriptive roles that TNMT plays such as pathway leading to the formation of different substrates including Protoberberine. <ref>20069275 </ref>
= Structural Highlights =
This protein has a <scene name='82/829888/Catalytic_triad/7'>catalytic triad</scene> which consists of amino acids His-208, Glu-204, and Glu-207. The authors explained within the paper that other amino acids may play a role in the triad as well. They were unsure but those three were the most accurate. These amino acids play an important role in catalysis for the protein. <ref> 20069275 </ref> The basic <scene name='82/829888/Spacefill_view_of_protein/1'>spacefill view</scene> of the entire protein alllows readers to visualize the different elements show in different colors. The elements shown are carbons(grey), nitrogen(blue), and oxygen(red). This protein has a <scene name='82/829888/Ligand/1'>Ligand</scene> which is SAM. There are <scene name='82/829888/Hydrophilic_side_chains/1'>hydrophilic side chains</scene>of SAM that form a small catalytic pocket and surrounds the amino group and methyl donor of SAM. This catalytic pocket forms a L shape. In green Glu-204, yellow is Glu-207, red is His-208, and Tyr-81 is blue.
<scene name='82/829888/Active_site/3'>Active Site</scene> This scene displays the active site of my the protein. In green, there is Alanine, in yellow Aspartic Acid, and in blue, Valine.

</StructureSection>

== References ==

Tetrahydroprotoberberine N-methyltransferase

2019-11-30T15:37:48Z

Deja Sanders:

= Structure =
<StructureSection load='6P3N' size='340' side='right' caption='Tetrahydroprotoberbine' scene=''>
'''Tetrahydroprotoberbine N-methyltransferase''' is a protein thats dimer interface includes six salt 6 salt bridges and 8 hydrogens bonds. It is expressed in E. ''coli'' and crystallized at a pH of 7.0. The crystals were grown in the presence of SAH,SAM, and SAH+SMS. Below are the two different substrates that were in the presence of the crystallized protein. The substrate SAM is shown to the right.
[[Image:6p3o.pdb1-500.jpg]]
[[Image:6p3m.pdb1-500.jpg]]
= Function =
The protein being studied, Tetrahydroprotoberbine N-methyltransferase, is found in yellow horned poppy (''Glaucium Flavum''). The function of the protein is substate recognition as well as catalysis for the ration engineering of enyzmes for chemoenzymatic synthesis and metabolic engineering. The relative activity of about 8 substrates were tested wiht Protoberberine having the highest percentage. GfTNMT's activity depends on temperature and pH. When the enzyme's activity was at a pH of 8, dropped 10% in activity. 10% activity was also dropped when the temperature was at 30 degrees Celsius. When at 4 degrees Celsius, the activity dropped even more down to 40%.
= Mutants =
In TMNT, three amino acid residues in the alpha14-helix form one side of the <scene name='82/829888/Binding_pocket/1'>binding pocket</scene> defining the BP region. The binding pocket consists of His-328(green), Ile-329(purple), and Phe-332(orange). The H328 mutation decreases in activity with stylopine and scoulerine producing a 5- and 2-fold while the activity with THP increases 2-fold.
= Relevance =
Studying Tetrahydroprotoberbine will provide commercial application where one will gain a lot of knowledge from both the research paper and online sources. Studying this protein will allow readers to engage in the material and apply their own knowledge to better understand the study. This research will provide descriptive roles that TNMT plays such as pathway leading to the formation of different substrates including Protoberberine. <ref>20069275 </ref>
= Structural Highlights =
This protein has a <scene name='82/829888/Catalytic_triad/7'>catalytic triad</scene> which consists of amino acids His-208, Glu-204, and Glu-207. The authors explained within the paper that other amino acids may play a role in the triad as well. They were unsure but those three were the most accurate. These amino acids play an important role in catalysis for the protein. <ref> 20069275 </ref> The basic <scene name='82/829888/Spacefill_view_of_protein/1'>spacefill view</scene> of the entire protein alllows readers to visualize the different elements show in different colors. The elements shown are carbons(grey), nitrogen(blue), and oxygen(red). This protein has a <scene name='82/829888/Ligand/1'>Ligand</scene> which is SAM. There are <scene name='82/829888/Hydrophillic_side_chains/1'>hydrophilic side chains</scene>of SAM that form a small catalytic pocket and surrounds the amino group and methyl donor of SAM. This catalytic pocket forms a L shape.
<scene name='82/829888/Active_site/3'>Active Site</scene> This scene displays the active site of my the protein. In green, there is Alanine, in yellow Aspartic Acid, and in blue, Valine.

</StructureSection>

== References ==

Tetrahydroprotoberberine N-methyltransferase

2019-11-30T15:23:09Z

Deja Sanders:

Tetrahydroprotoberberine N-methyltransferase

2019-11-30T14:52:55Z

Deja Sanders:

Tetrahydroprotoberberine N-methyltransferase

2019-11-30T05:55:58Z

Deja Sanders:

Tetrahydroprotoberberine N-methyltransferase

2019-11-30T05:54:56Z

Deja Sanders:

Tetrahydroprotoberberine N-methyltransferase

2019-11-30T05:53:37Z

Deja Sanders:

File:6p3o.pdb1-500.jpg

2019-11-30T05:52:31Z

Deja Sanders:

File:6p3m.pdb1-500.jpg

2019-11-30T05:47:25Z

Deja Sanders:

Tetrahydroprotoberberine N-methyltransferase

2019-11-30T05:39:16Z

Deja Sanders:

Tetrahydroprotoberberine N-methyltransferase

2019-11-30T05:38:32Z

Deja Sanders:

= Structure =
<StructureSection load='6P3N' size='340' side='right' caption='Tetrahydroprotoberbine' scene=''>
'''Tetrahydroprotoberbine N-methyltransferase''' is a protein thats dimer interface includes six salt 6 salt bridges and 8 hydrogens bonds. It is expressed in E. ''coli'' and crystallized at a pH of 7.0. The crystals were grown in the presence of SAH,SAM, and SAH+SMS. Below are all three different substrates that were in the presence of the crystallized protein. <Structure load='6p3m' size='300' frame='true' align='right' caption='GfTNMT + SAH' scene='GfTNMT + SAH' /> <Structure load='6P3N' size='300' frame='true' align='right' caption='GfTNMT + SAM' scene='GfTNMT + SAM' /> <Structure load='6P3O' size='300' frame='true' align='right' caption='GfTNMT + SAH + SMS' scene='GfTNMT + SAH + SMS' />
= Function =
The protein being studied, Tetrahydroprotoberbine N-methyltransferase, is found in yellow horned poppy (''Glaucium Flavum''). The function of the protein is substate recognition as well as catalysis for the ration engineering of enyzmes for chemoenzymatic synthesis and metabolic engineering. The relative activity of about 8 substrates were tested wiht Protoberberine having the highest percentage. GfTNMT's activity depends on temperature and pH. When the enzyme's activity was at a pH of 8, dropped 10% in activity. 10% activity was also dropped when the temperature was at 30 degrees Celsius. When at 4 degrees Celsius, the activity dropped even more down to 40%.
= Mutants =
In TMNT, three amino acid residues in the alpha14-helix form one side of the <scene name='82/829888/Binding_pocket/1'>binding pocket</scene> defining the BP region. The binding pocket consists of His-328(green), Ile-329(purple), and Phe-332(orange). The H328 mutation decreases in activity with stylopine and scoulerine producing a 5- and 2-fold while the activity with THP increases 2-fold.
= Relevance =
Studying Tetrahydroprotoberbine will provide commercial application where one will gain a lot of knowledge from both the research paper and online sources. Studying this protein will allow readers to engage in the material and apply their own knowledge to better understand the study. This research will provide descriptive roles that TNMT plays such as pathway leading to the formation of different substrates including Protoberberine. <ref>20069275 </ref>
= Structural Highlights =
<scene name='82/829888/Catalytic_triad/6'>Catalytic Triad</scene> This scene displays the catalytic triad which are the amino acids His-208, Glu-204, and Glu-207. The authors explained within the paper that other amino acids may play a role in the triad as well. They were unsure but those three were the most accurate. These amino acids play an important role in catalysis for the protein.

<scene name='82/829888/Spacefill_view_of_protein/1'>Spacefill View of Protein</scene> This scene displays the spacefill view of Tetrahydroprotoberbine. This view allows viewers to see the different colored elements such as carbon(grey), nitrogen(blue), and oxygen(red).

<scene name='82/829888/Ligand/1'>Ligand</scene> This scene displays the ligand of the protein. The ligand of the protein is named SAM.

<scene name='82/829888/Active_site/3'>Active Site</scene> This scene displays the active site of my the protein. In green, there is Alanine, in yellow Asparatic Acid, and in blue Valine.

</StructureSection>

== References ==
<references/>

Tetrahydroprotoberberine N-methyltransferase

2019-11-30T05:23:52Z

Deja Sanders:

Tetrahydroprotoberberine N-methyltransferase

2019-11-30T05:16:15Z

Deja Sanders:

= Structure =
<StructureSection load='6P3N' size='340' side='right' caption='Tetrahydroprotoberbine' scene=''>
'''Tetrahydroprotoberbine N-methyltransferase''' is a protein that was expressed in E. ''coli'' and crystallized at a pH of 7.0. The crystals were grown in the presence of SAH,SAM, and SAH+SMS. The dimer interface includes six salt 6 salt bridges and 8 hydrogens bonds.

= Function =
The protein being studied, Tetrahydroprotoberbine N-methyltransferase, is found in yellow horned poppy (''Glaucium Flavum''). The function of the protein is substate recognition as well as catalysis for the ration engineering of enyzmes for chemoenzymatic synthesis and metabolic engineering. The relative activity of about 8 substrates were tested wiht Protoberberine having the highest percentage. GfTNMT's activity depends on temperature and pH. When the enzyme's activity was at a pH of 8, dropped 10% in activity. 10% activity was also dropped when the temperature was at 30 degrees Celsius. When at 4 degrees Celsius, the activity dropped even more down to 40%.
= Mutants =
= Relevance =
Studying Tetrahydroprotoberbine will provide commercial application where one will gain a lot of knowledge from both the research paper and online sources. Studying this protein will allow readers to engage in the material and apply their own knowledge to better understand the study. This research will provide descriptive roles that TNMT plays such as pathway leading to the formation of different substrates including Protoberberine. <ref>20069275 </ref>
= Structural Highlights =
<scene name='82/829888/Catalytic_triad/6'>Catalytic Triad</scene> This scene displays the catalytic triad which are the amino acids His-208, Glu-204, and Glu-207. The authors explained within the paper that other amino acids may play a role in the triad as well. They were unsure but those three were the most accurate. These amino acids play an important role in catalysis for the protein.

<scene name='82/829888/Spacefill_view_of_protein/1'>Spacefill View of Protein</scene> This scene displays the spacefill view of Tetrahydroprotoberbine. This view allows viewers to see the different colored elements such as carbon(grey), nitrogen(blue), and oxygen(red).

<scene name='82/829888/Ligand/1'>Ligand</scene> This scene displays the ligand of the protein. The ligand of the protein is named SAM.

<scene name='82/829888/Active_site/3'>Active Site</scene> This scene displays the active site of my the protein. In green, there is Alanine, in yellow Asparatic Acid, and in blue Valine.

</StructureSection>

== References ==
<references/>

Tetrahydroprotoberberine N-methyltransferase

2019-11-30T05:13:59Z

Deja Sanders:

==Structure==
<StructureSection load='6P3N' size='340' side='right' caption='Tetrahydroprotoberbine' scene=''>
'''Tetrahydroprotoberbine N-methyltransferase''' is a protein that was expressed in E. ''coli'' and crystallized at a pH of 7.0. The crystals were grown in the presence of SAH,SAM, and SAH+SMS. The dimer interface includes six salt 6 salt bridges and 8 hydrogens bonds.

== Function ==
The protein being studied, Tetrahydroprotoberbine N-methyltransferase, is found in yellow horned poppy (''Glaucium Flavum''). The function of the protein is substate recognition as well as catalysis for the ration engineering of enyzmes for chemoenzymatic synthesis and metabolic engineering. The relative activity of about 8 substrates were tested wiht Protoberberine having the highest percentage. GfTNMT's activity depends on temperature and pH. When the enzyme's activity was at a pH of 8, dropped 10% in activity. 10% activity was also dropped when the temperature was at 30 degrees Celsius. When at 4 degrees Celsius, the activity dropped even more down to 40%.
= Mutants =

== Relevance ==
Studying Tetrahydroprotoberbine will provide commercial application where one will gain a lot of knowledge from both the research paper and online sources. Studying this protein will allow readers to engage in the material and apply their own knowledge to better understand the study. This research will provide descriptive roles that TNMT plays such as pathway leading to the formation of different substrates including Protoberberine. <ref>20069275 </ref>
= Structural highlights =
<scene name='82/829888/Catalytic_triad/6'>Catalytic Triad</scene> This scene displays the catalytic triad which are the amino acids His-208, Glu-204, and Glu-207. The authors explained within the paper that other amino acids may play a role in the triad as well. They were unsure but those three were the most accurate. These amino acids play an important role in catalysis for the protein.

<scene name='82/829888/Spacefill_view_of_protein/1'>Spacefill View of Protein</scene> This scene displays the spacefill view of Tetrahydroprotoberbine. This view allows viewers to see the different colored elements such as carbon(grey), nitrogen(blue), and oxygen(red).

<scene name='82/829888/Ligand/1'>Ligand</scene> This scene displays the ligand of the protein. The ligand of the protein is named SAM.

<scene name='82/829888/Active_site/3'>Active Site</scene> This scene displays the active site of my the protein. In green, there is Alanine, in yellow Asparatic Acid, and in blue Valine.

</StructureSection>

== References ==
<references/>

Tetrahydroprotoberberine N-methyltransferase

2019-11-30T05:00:23Z

Deja Sanders:

==Structure==
<StructureSection load='6P3N' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Tetrahydroprotoberbine N-methyltransferase Protein'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==
The protein being studied, Tetrahydroprotoberbine N-methyltransferase, is found in yellow horned poppy (''Glaucium Flavum''). The function of the protein is substate recognition as well as catalysis for the ration engineering of enyzmes for chemoenzymatic synthesis and metabolic engineering. The relative activity of about 8 substrates were tested wiht Protoberberine having the highest percentage. GfTNMT's activity depends on temperature and pH. When the enzyme's activity was at a pH of 8, dropped 10% in activity. 10% activity was also dropped when the temperature was at 30 degrees Celsius. When at 4 degrees Celsius, the activity dropped even more down to 40%.
= Mutants =

== Relevance ==
Studying Tetrahydroprotoberbine will provide commercial application where one will gain a lot of knowledge from both the research paper and online sources. Studying this protein will allow readers to engage in the material and apply their own knowledge to better understand the study. This research will provide descriptive roles that TNMT plays such as pathway leading to the formation of different substrates including Protoberberine. <ref>20069275 </ref>
= Structural highlights =
<scene name='82/829888/Catalytic_triad/6'>Catalytic Triad</scene> This scene displays the catalytic triad which are the amino acids His-208, Glu-204, and Glu-207. The authors explained within the paper that other amino acids may play a role in the triad as well. They were unsure but those three were the most accurate. These amino acids play an important role in catalysis for the protein.

<scene name='82/829888/Spacefill_view_of_protein/1'>Spacefill View of Protein</scene> This scene displays the spacefill view of Tetrahydroprotoberbine. This view allows viewers to see the different colored elements such as carbon(grey), nitrogen(blue), and oxygen(red).

<scene name='82/829888/Ligand/1'>Ligand</scene> This scene displays the ligand of the protein. The ligand of the protein is named SAM.

<scene name='82/829888/Active_site/3'>Active Site</scene> This scene displays the active site of my the protein. In green, there is Alanine, in yellow Asparatic Acid, and in blue Valine.

</StructureSection>

== References ==
<references/>

Tetrahydroprotoberberine N-methyltransferase

2019-11-30T04:46:32Z

Deja Sanders:

==Structure==
<StructureSection load='6P3N' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Tetrahydroprotoberbine N-methyltransferase Protein'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==
The protein being studied, Tetrahydroprotoberbine N-methyltransferase, is found in yellow horned poppy (''Glaucium Flavum''). The function of the protein is substate recognition as well as catalysis for the ration engineering of enyzmes for chemoenzymatic synthesis and metabolic engineering. The relative activity of 8 and more substrates were tested. Protoberberine had the highest percentage.
= Disease =

== Relevance ==
Studying Tetrahydroprotoberbine will provide commercial application where one will gain a lot of knowledge from both the research paper and online sources. Studying this protein will allow readers to engage in the material and apply their own knowledge to better understand the study. This research will provide descriptive roles that TNMT plays such as pathway leading to the formation of different substrates including Protoberberine. <ref>20069275 </ref>
= Structural highlights =
<scene name='82/829888/Catalytic_triad/6'>Catalytic Triad</scene> This scene displays the catalytic triad which are the amino acids His-208, Glu-204, and Glu-207. The authors explained within the paper that other amino acids may play a role in the triad as well. They were unsure but those three were the most accurate. These amino acids play an important role in catalysis for the protein.

<scene name='82/829888/Spacefill_view_of_protein/1'>Spacefill View of Protein</scene> This scene displays the spacefill view of Tetrahydroprotoberbine. This view allows viewers to see the different colored elements such as carbon(grey), nitrogen(blue), and oxygen(red).

<scene name='82/829888/Ligand/1'>Ligand</scene> This scene displays the ligand of the protein. The ligand of the protein is named SAM.

<scene name='82/829888/Active_site/3'>Active Site</scene> This scene displays the active site of my the protein. In green, there is Alanine, in yellow Asparatic Acid, and in blue Valine.

</StructureSection>

== References ==
<references/>

Tetrahydroprotoberberine N-methyltransferase

2019-11-28T02:15:04Z

Deja Sanders:

==Structure==
<StructureSection load='6P3N' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Tetrahydroprotoberbine N-methyltransferase Protein'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==
The protein being studied, Tetrahydroprotoberbine N-methyltransferase, is found in yellow horned poppy (''Glaucium Flavum''). The function of the protein is substate recognition as well as catalysis for the ration engineering of enyzmes for chemoenzymatic synthesis and metabolic engineering. The relative activity of 8 and more substrates were tested. Protoberberine had the highest percentage.
= Disease =

== Relevance ==
Studying Tetrahydroprotoberbine will provide commercial application where one will gain a lot of knowledge from both the research paper and online sources. Studying this protein will allow readers to engage in the material and apply their own knowledge to better understand the study. This research will provide descriptive roles that TNMT plays such as pathway leading to the formation of different substrates including Protoberberine. <ref>20069275 </ref>
= Structural highlights =
<scene name='82/829888/Catalytic_triad/6'>Catalytic Triad</scene> This scene displays the catalytic triad which are the amino acids His-208, Glu-204, and Glu-207. The authors explained within the paper that other amino acids may play a role in the triad as well. They were unsure but those three were the most accurate. These amino acids play an important role in catalysis for the protein.

<scene name='82/829888/Spacefill_view_of_protein/1'>Spacefill View of Protein</scene> This scene displays the spacefill view of Tetrahydroprotoberbine. This view allows viewers to see the different colored elements such as carbon(grey), nitrogen(blue), and oxygen(red).

<scene name='82/829888/Ligand/1'>Ligand</scene> This scene displays the ligand of the protein. The ligand of the protein is named SAM.

</StructureSection>

== References ==
<references/>

Tetrahydroprotoberberine N-methyltransferase

2019-11-28T01:45:29Z

Deja Sanders:

==Structure==
<StructureSection load='6P3N' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Tetrahydroprotoberbine N-methyltransferase Protein'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==
The protein being studied, Tetrahydroprotoberbine N-methyltransferase, is found in yellow horned poppy (''Glaucium Flavum''). The function of the protein is substate recognition as well as catalysis for the ration engineering of enyzmes for chemoenzymatic synthesis and metabolic engineering. The relative activity of 8 and more substrates were tested. Protoberberine had the highest percentage.
= Disease =

== Relevance ==
Studying Tetrahydroprotoberbine will provide commercial application where one will gain a lot of knowledge from both the research paper and online sources. Studying this protein will allow readers to engage in the material and apply their own knowledge to better understand the study. This research will provide descriptive roles that TNMT plays such as pathway leading to the formation of different substrates including Protoberberine. <ref>20069275 </ref>
= Structural highlights =
<scene name='82/829888/Catalytic_triad/6'>Catalytic Triad</scene> This scene displays the catalytic triad which are the amino acids His-208, Glu-204, and Glu-207. The authors explained within the paper that other amino acids may play a role in the triad as well. They were unsure but those three were the most accurate. These amino acids play an important role in catalysis for the protein.

<scene name='82/829888/Spacefill_view_of_protein/1'>Spacefill View of Protein</scene> This scene displays the spacefill view of Tetrahydroprotoberbine. This view allows viewers to see the different colored elements such as carbon(grey), nitrogen(blue), and oxygen(red).

</StructureSection>

== References ==
<references/>

Tetrahydroprotoberberine N-methyltransferase

2019-11-28T01:39:51Z

Deja Sanders:

==Structure==
<StructureSection load='6P3N' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Tetrahydroprotoberbine N-methyltransferase Protein'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==
The protein being studied, Tetrahydroprotoberbine N-methyltransferase, is found in yellow horned poppy (''Glaucium Flavum''). The function of the protein is substate recognition as well as catalysis for the ration engineering of enyzmes for chemoenzymatic synthesis and metabolic engineering. The relative activity of 8 and more substrates were tested. Protoberberine had the highest percentage.
= Disease =

== Relevance ==
Studying Tetrahydroprotoberbine will provide commercial application where one will gain a lot of knowledge from both the research paper and online sources. Studying this protein will allow readers to engage in the material and apply their own knowledge to better understand the study. This research will provide descriptive roles that TNMT plays such as pathway leading to the formation of different substrates including Protoberberine. <ref> 20069275 </ref)
= Structural highlights =
<scene name='82/829888/Catalytic_triad/6'>Catalytic Triad</scene> This scene displays the catalytic triad which are the amino acids His-208, Glu-204, and Glu-207. The authors explained within the paper that other amino acids may play a role in the triad as well. They were unsure but those three were the most accurate. These amino acids play an important role in catalysis for the protein.

<scene name='82/829888/Spacefill_view_of_protein/1'>Spacefill View of Protein</scene> This scene displays the spacefill view of Tetrahydroprotoberbine. This view allows viewers to see the different colored elements such as carbon(grey), nitrogen(blue), and oxygen(red).
</StructureSection>
== References ==
<references/>

Tetrahydroprotoberberine N-methyltransferase

2019-11-28T01:02:19Z

Deja Sanders:

Tetrahydroprotoberberine N-methyltransferase

2019-11-28T00:57:20Z

Deja Sanders:

Tetrahydroprotoberberine N-methyltransferase

2019-11-28T00:53:34Z

Deja Sanders:

==Your Heading Here (maybe something like 'Structure')==
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Tetrahydroprotoberbine N-methyltransferase Protein'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==

== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

Tetrahydroprotoberberine N-methyltransferase

2019-11-28T00:48:36Z

Deja Sanders:

==Structure==
<StructureSection load='6P3N' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Tetrahydroprotoberbine N-methyltransferase'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==
The protein being studied, Tetrahydroprotoberbine N-methyltransferase, is found in yellow horned poppy (''Glaucium Flavum''). The function of the protein is substate recognition as well as catalysis for the ration engineering of enyzmes for chemoenzymatic synthesis and metabolic engineering. The relative activity of 8 and more substrates were tested. Protoberberine had the highest percentage.
== Disease ==

== Relevance ==
Studying Tetrahydroprotoberbine will provide commercial application where one will gain a lot of knowledge from both the research paper and online sources. Studying this protein will allow readers to engage in the material and apply their own knowledge to better understand the study. This research will provide descriptive roles that TNMT plays such as pathway leading to the formation of different substrates including Protoberberine. <ref> 20069275 </ref)

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

This scene displays the catalytic triad which are the amino acids His-208, Glu-204, and Glu-207. The authors explained within the paper that other amino acids may play a role in the triad as well. They were unsure but those three were the most accurate. These amino acids play an important role in catalysis for the protein.
== References ==
<references/>

Tetrahydroprotoberberine N-methyltransferase

2019-11-28T00:39:47Z

Deja Sanders:

Tetrahydroprotoberberine N-methyltransferase

2019-11-28T00:39:14Z

Deja Sanders:

Tetrahydroprotoberberine N-methyltransferase

2019-11-28T00:38:52Z

Deja Sanders:

Tetrahydroprotoberberine N-methyltransferase

2019-11-28T00:38:02Z

Deja Sanders:

Tetrahydroprotoberberine N-methyltransferase

2019-11-28T00:36:08Z

Deja Sanders:

Tetrahydroprotoberberine N-methyltransferase

2019-11-28T00:18:40Z

Deja Sanders:

Tetrahydroprotoberberine N-methyltransferase

2019-11-28T00:17:37Z

Deja Sanders: