Sandbox Reserved 1567: Difference between revisions

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= Structure =
= Structure =
<StructureSection load='6P3N' size='340' side='right' caption='Tetrahydroprotoberbine' scene=''>
<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.   
'''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.   
[[Image:6p3o.pdb1-500.jpg]]
 
[[Image:6p3m.pdb1-500.jpg]]
= Function =
= 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%.  
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%.