Proteopedia - User contributions [en]

Sandbox Reserved 1763&action=edit

2022-12-13T19:02:46Z

Carmen J Almendarez Rodriguez:

==Human Orthinine Aminotransferase (hOAT)==
<StructureSection load='7t9z' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Sandbox Reserved 1763&action=edit'''. 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 Orthinine Aminotransferase (OAT) <ref>35460691</ref>. and hOAT in humans is an enzyme that catalyzes the transfer of an amino acid group L-orthinine from L-orthinine to an alpha-ketoglutarate. Its ligand pyrodixal-5-phosphate (PLP) is a cofactor in the reaction. An amino group from L-orthinine is transferred to PLP which converts it to pyridoxamine phosphate (PMP) and L-orthinine is converted to L-glutamate-y-semialdehyde. PLP is regenerated when PMP is transferred to alpha-KG.
== Bilogical relavance and broader implications ==
hOAT is an enzyme that is found in almost all tissues but predominately in the liver and kidney. There is an overexpression of hOAT in cancer cells so understanding it can help the proliferation of cancer cells, especially hepatocellular carcinoma (HCC) which is a type of liver cell. hOAT has been a target mechanism-based inactivator (MBIs) in an attempt to create drugs. HCC is generally diagnosed in advanced stages which makes cancer more resistant to chemotherapy. hOAT inhibitors were created as fragmented-sized alternative substrates such as y-aminobutyric acid (GABA) and 5-aminovaleric acid (AVA). GABA is covalently bonded to PLP. While AVA is covalently attached to PLP by lysine 292, which is a catalytic enzyme in the binding pocket. GABA and AVA have strong binding affinity but slow turnovers.
== Important amino acids ==
The amino acids in the PLP binding site are <scene name='94/941534/Lysine_292/1'>Lys 292</scene>, <scene name='94/941534/Aspartate_263/1'>Asp 263</scene>, <scene name='94/941534/Arginine_180/1'>Arg 180</scene>, and <scene name='94/941534/Phe_177/1'>Phe 177</scene>. They are essential in the active site because of their interaction with PLP. PLP is covalently bonded to the amino acid lysine. The nitrogen in the ring of PLP interacts with the negatively charged oxygen in the aspartate side chain. The phosphate interacts with the positively charged nitrogen of the arginine side chain. And Phe 177 has a pi- stacking interaction between its ring and the ring of PLP
== Structural highlights ==
hOAT is a protein with a <scene name='94/941534/Secondary_structure/1'>secondary structure</scene> that is mainly made of alpha helices but also has parallel and anti-parallel beta sheets and random coil. Its a polymer with a <scene name='94/941534/Globular_module/1'>globular structure</scene> that has three subunits held by non-cavantly interactions like hydrogen bond and salt bridges between the side chains and amino acids. The binding pocket is semi-exposed which makes helps competitive substrates bind to the active site. The PLP has a phosphate groups surrounded by polar amino acids and the carbons are surrounded by non-polar amino acids which makes it favorable for the ligand and active site. PLP has polar (hydrophilic) portions that are exposed to the surrounding and non-polar (hydophobic) protions that are hidden within the protein making it stable. Hydrogen bonding and pi-stacking stabilize the <scene name='94/941534/Ligand_of_interest/1'>ligand</scene> and the active site.
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/>

Sandbox Reserved 1763&action=edit

2022-12-13T19:00:38Z

Carmen J Almendarez Rodriguez:

Sandbox Reserved 1763&action=edit

2022-12-13T18:48:40Z

Carmen J Almendarez Rodriguez:

==Human Orthinine Aminotransferase (hOAT)==
<StructureSection load='7t9z' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Sandbox Reserved 1763&action=edit'''. 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 Orthinine Aminotransferase (OAT) and hOAT in humans is an enzyme that catalyzes the transfer of an amino acid group L-orthinine from L-orthinine to an alpha-ketoglutarate. Its ligand pyrodixal-5-phosphate (PLP) is a cofactor in the reaction. An amino group from L-orthinine is transferred to PLP which converts it to pyridoxamine phosphate (PMP) and L-orthinine is converted to L-glutamate-y-semialdehyde. PLP is regenerated when PMP is transferred to alpha-KG.
== Bilogical relavance and broader implications ==
hOAT is an enzyme that is found in almost all tissues but predominately in the liver and kidney. There is an overexpression of hOAT in cancer cells so understanding it can help the proliferation of cancer cells, especially hepatocellular carcinoma (HCC) which is a type of liver cell. hOAT has been a target mechanism-based inactivator (MBIs) in an attempt to create drugs. HCC is generally diagnosed in advanced stages which makes cancer more resistant to chemotherapy. hOAT inhibitors were created as fragmented-sized alternative substrates such as y-aminobutyric acid (GABA) and 5-aminovaleric acid (AVA). GABA is covalently bonded to PLP. While AVA is covalently attached to PLP by lysine 292, which is a catalytic enzyme in the binding pocket. GABA and AVA have strong binding affinity but slow turnovers.
== Important amino acids ==
The amino acids in the PLP binding site are <scene name='94/941534/Lysine_292/1'>Lys 292</scene>, <scene name='94/941534/Aspartate_263/1'>Asp 263</scene>, <scene name='94/941534/Arginine_180/1'>Arg 180</scene>, and <scene name='94/941534/Phe_177/1'>Phe 177</scene>. They are essential in the active site because of their interaction with PLP. PLP is covalently bonded to the amino acid lysine. The nitrogen in the ring of PLP interacts with the negatively charged oxygen in the aspartate side chain. The phosphate interacts with the positively charged nitrogen of the arginine side chain. And Phe 177 has a pi- stacking interaction between its ring and the ring of PLP
== Structural highlights ==
hOAT is a protein with a <scene name='94/941534/Secondary_structure/1'>secondary structure</scene> that is mainly made of alpha helices but also has parallel and anti-parallel beta sheets and random coil. Its a polymer with a <scene name='94/941534/Globular_module/1'>globular structure</scene> that has three subunits held by non-cavantly interactions like hydrogen bond and salt bridges between the side chains and amino acids. The binding pocket is semi-exposed which makes helps competitive substrates bind to the active site. The PLP has a phosphate groups surrounded by polar amino acids and the carbons are surrounded by non-polar amino acids which makes it favorable for the ligand and active site. PLP has polar (hydrophilic) portions that are exposed to the surrounding and non-polar (hydophobic) protions that are hidden within the protein making it stable. Hydrogen bonding and pi-stacking stabilize the <scene name='94/941534/Ligand_of_interest/1'>ligand</scene> and the active site.
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/>

Sandbox Reserved 1763&action=edit

2022-12-13T18:45:52Z

Carmen J Almendarez Rodriguez:

==Human Orthinine Aminotransferase (hOAT)==
<StructureSection load='7t9z' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Sandbox Reserved 1763&action=edit'''. 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 Orthinine Aminotransferase (OAT) and hOAT in humans is an enzyme that catalyzes the transfer of an amino acid group L-orthinine from L-orthinine to an alpha-ketoglutarate. Its ligand pyrodixal-5-phosphate (PLP) is a cofactor in the reaction. An amino group from L-orthinine is transferred to PLP which converts it to pyridoxamine phosphate (PMP) and L-orthinine is converted to L-glutamate-y-semialdehyde. PLP is regenerated when PMP is transferred to alpha-KG.
== Bilogical relavance and broader implications ==
hOAT is an enzyme that is found in almost all tissues but predominately in the liver and kidney. There is an overexpression of hOAT in cancer cells so understanding it can help the proliferation of cancer cells, especially hepatocellular carcinoma (HCC) which is a type of liver cell. hOAT has been a target mechanism-based inactivator (MBIs) in an attempt to create drugs. HCC is generally diagnosed in advanced stages which makes cancer more resistant to chemotherapy. hOAT inhibitors were created as fragmented-sized alternative substrates such as y-aminobutyric acid (GABA) and 5-aminovaleric acid (AVA). GABA is covalently bonded to PLP. While AVA is covalently attached to PLP by lysine 292, which is a catalytic enzyme in the binding pocket. GABA and AVA have strong binding affinity but slow turnovers.
== Important amino acids ==
The amino acids in the PLP binding site are <scene name='94/941534/Lysine_292/1'>Lys 292</scene>, <scene name='94/941534/Aspartate_263/1'>Asp 263</scene>, <scene name='94/941534/Arginine_180/1'>Arg 180</scene>, and <scene name='94/941534/Phe_177/1'>Phe 177</scene>. They are essential in the active site because of their interaction with PLP. PLP is covalently bonded to the amino acid lysine. The nitrogen in the ring of PLP interacts with the negatively charged oxygen in the aspartate side chain. The phosphate interacts with the positively charged nitrogen of the arginine side chain. And Phe 177 has a pi- stacking interaction between its ring and the ring of PLP
== Structural highlights ==
hOAT is a protein with a secondary structure that is mainly made of alpha helices but also has parallel and anti-parallel beta sheets and random coil. Its a polymer with a <scene name='94/941534/Globular_module/1'>globular structure</scene> that has three subunits held by non-cavantly interactions like hydrogen bond and salt bridges between the side chains and amino acids. The binding pocket is semi-exposed which makes helps competitive substrates bind to the active site. The PLP has a phosphate groups surrounded by polar amino acids and the carbons are surrounded by non-polar amino acids which makes it favorable for the ligand and active site. PLP has polar (hydrophilic) portions that are exposed to the surrounding and non-polar (hydophobic) protions that are hidden within the protein making it stable. Hydrogen bonding and pi-stacking stabilize the <scene name='94/941534/Ligand_of_interest/1'>ligand</scene> and the active site.
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/>

Sandbox Reserved 1763&action=edit

2022-12-13T18:43:11Z

Carmen J Almendarez Rodriguez:

==Human Orthinine Aminotransferase (hOAT)==
<StructureSection load='7t9z' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Sandbox Reserved 1763&action=edit'''. 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 Orthinine Aminotransferase (OAT) and hOAT in humans is an enzyme that catalyzes the transfer of an amino acid group L-orthinine from L-orthinine to an alpha-ketoglutarate. Its ligand pyrodixal-5-phosphate (PLP) is a cofactor in the reaction. An amino group from L-orthinine is transferred to PLP which converts it to pyridoxamine phosphate (PMP) and L-orthinine is converted to L-glutamate-y-semialdehyde. PLP is regenerated when PMP is transferred to alpha-KG.
== Bilogical relavance and broader implications ==
hOAT is an enzyme that is found in almost all tissues but predominately in the liver and kidney. There is an overexpression of hOAT in cancer cells so understanding it can help the proliferation of cancer cells, especially hepatocellular carcinoma (HCC) which is a type of liver cell. hOAT has been a target mechanism-based inactivator (MBIs) in an attempt to create drugs. HCC is generally diagnosed in advanced stages which makes cancer more resistant to chemotherapy. hOAT inhibitors were created as fragmented-sized alternative substrates such as y-aminobutyric acid (GABA) and 5-aminovaleric acid (AVA). GABA is covalently bonded to PLP. While AVA is covalently attached to PLP by lysine 292, which is a catalytic enzyme in the binding pocket. GABA and AVA have strong binding affinity but slow turnovers.
== Important amino acids ==
The amino acids in the PLP binding site are <scene name='94/941534/Lysine_292/1'>Lys 292</scene>, <scene name='94/941534/Aspartate_263/1'>Asp 263</scene>, <scene name='94/941534/Arginine_180/1'>Arg 180</scene>, and <scene name='94/941534/Phe_177/1'>Phe 177</scene>. They are essential in the active site because of their interaction with PLP. PLP is covalently bonded to the amino acid lysine. The nitrogen in the ring of PLP interacts with the negatively charged oxygen in the aspartate side chain. The phosphate interacts with the positively charged nitrogen of the arginine side chain. And Phe 177 has a pi- stacking interaction between its ring and the ring of PLP
== Structural highlights ==
hOAT is a protein with a secondary structure that is mainly made of alpha helices but also has parallel and anti-parallel beta sheets and random coil. Its a polymer with a globular structure that has three subunits held by non-cavantly interactions like hydrogen bond and salt bridges between the side chains and amino acids. The binding pocket is semi-exposed which makes helps competitive substrates bind to the active site. The PLP has a phosphate groups surrounded by polar amino acids and the carbons are surrounded by non-polar amino acids which makes it favorable for the ligand and active site. PLP has polar (hydrophilic) portions that are exposed to the surrounding and non-polar (hydophobic) protions that are hidden within the protein making it stable. Hydrogen bonding and pi-stacking stabilize the <scene name='94/941534/Ligand_of_interest/1'>ligand</scene> and the active site.
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/>

Sandbox Reserved 1763&action=edit

2022-12-13T18:39:19Z

Carmen J Almendarez Rodriguez:

==Human Orthinine Aminotransferase (hOAT)==
<StructureSection load='7t9z' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Sandbox Reserved 1763&action=edit'''. 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 Orthinine Aminotransferase (OAT) and hOAT in humans is an enzyme that catalyzes the transfer of an amino acid group L-orthinine from L-orthinine to an alpha-ketoglutarate. Its ligand pyrodixal-5-phosphate (PLP) is a cofactor in the reaction. An amino group from L-orthinine is transferred to PLP which converts it to pyridoxamine phosphate (PMP) and L-orthinine is converted to L-glutamate-y-semialdehyde. PLP is regenerated when PMP is transferred to alpha-KG.
== Bilogical relavance and broader implications ==
hOAT is an enzyme that is found in almost all tissues but predominately in the liver and kidney. There is an overexpression of hOAT in cancer cells so understanding it can help the proliferation of cancer cells, especially hepatocellular carcinoma (HCC) which is a type of liver cell. hOAT has been a target mechanism-based inactivator (MBIs) in an attempt to create drugs. HCC is generally diagnosed in advanced stages which makes cancer more resistant to chemotherapy. hOAT inhibitors were created as fragmented-sized alternative substrates such as y-aminobutyric acid (GABA) and 5-aminovaleric acid (AVA). GABA is covalently bonded to PLP. While AVA is covalently attached to PLP by lysine 292, which is a catalytic enzyme in the binding pocket. GABA and AVA have strong binding affinity but slow turnovers.
== Important amino acids ==
The amino acids in the PLP binding site are <scene name='94/941534/Lysine_292/1'>Lys 292</scene>, <scene name='94/941534/Aspartate_263/1'>Asp 263</scene>, <scene name='94/941534/Arginine_180/1'>Arg 180</scene>, and Phe 177. They are essential in the active site because of their interaction with PLP. PLP is covalently bonded to the amino acid lysine. The nitrogen in the ring of PLP interacts with the negatively charged oxygen in the aspartate side chain. The phosphate interacts with the positively charged nitrogen of the arginine side chain. And Phe 177 has a pi- stacking interaction between its ring and the ring of PLP
== Structural highlights ==
hOAT is a protein with a secondary structure that is mainly made of alpha helices but also has parallel and anti-parallel beta sheets and random coil. Its a polymer with a globular structure that has three subunits held by non-cavantly interactions like hydrogen bond and salt bridges between the side chains and amino acids. The binding pocket is semi-exposed which makes helps competitive substrates bind to the active site. The PLP has a phosphate groups surrounded by polar amino acids and the carbons are surrounded by non-polar amino acids which makes it favorable for the ligand and active site. PLP has polar (hydrophilic) portions that are exposed to the surrounding and non-polar (hydophobic) protions that are hidden within the protein making it stable. Hydrogen bonding and pi-stacking stabilize the <scene name='94/941534/Ligand_of_interest/1'>ligand</scene> and the active site.
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/>

Sandbox Reserved 1763&action=edit

2022-12-13T18:35:00Z

Carmen J Almendarez Rodriguez:

==Human Orthinine Aminotransferase (hOAT)==
<StructureSection load='7t9z' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Sandbox Reserved 1763&action=edit'''. 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 Orthinine Aminotransferase (OAT) and hOAT in humans is an enzyme that catalyzes the transfer of an amino acid group L-orthinine from L-orthinine to an alpha-ketoglutarate. Its ligand pyrodixal-5-phosphate (PLP) is a cofactor in the reaction. An amino group from L-orthinine is transferred to PLP which converts it to pyridoxamine phosphate (PMP) and L-orthinine is converted to L-glutamate-y-semialdehyde. PLP is regenerated when PMP is transferred to alpha-KG.
== Bilogical relavance and broader implications ==
hOAT is an enzyme that is found in almost all tissues but predominately in the liver and kidney. There is an overexpression of hOAT in cancer cells so understanding it can help the proliferation of cancer cells, especially hepatocellular carcinoma (HCC) which is a type of liver cell. hOAT has been a target mechanism-based inactivator (MBIs) in an attempt to create drugs. HCC is generally diagnosed in advanced stages which makes cancer more resistant to chemotherapy. hOAT inhibitors were created as fragmented-sized alternative substrates such as y-aminobutyric acid (GABA) and 5-aminovaleric acid (AVA). GABA is covalently bonded to PLP. While AVA is covalently attached to PLP by lysine 292, which is a catalytic enzyme in the binding pocket. GABA and AVA have strong binding affinity but slow turnovers.
== Important amino acids ==
The amino acids in the PLP binding site are <scene name='94/941534/Lysine_292/1'>Lys 292</scene>, <scene name='94/941534/Aspartate_263/1'>Asp 263</scene>, Arg 180, and Phe 177. They are essential in the active site because of their interaction with PLP. PLP is covalently bonded to the amino acid lysine. The nitrogen in the ring of PLP interacts with the negatively charged oxygen in the aspartate side chain. The phosphate interacts with the positively charged nitrogen of the arginine side chain. And Phe 177 has a pi- stacking interaction between its ring and the ring of PLP
== Structural highlights ==
hOAT is a protein with a secondary structure that is mainly made of alpha helices but also has parallel and anti-parallel beta sheets and random coil. Its a polymer with a globular structure that has three subunits held by non-cavantly interactions like hydrogen bond and salt bridges between the side chains and amino acids. The binding pocket is semi-exposed which makes helps competitive substrates bind to the active site. The PLP has a phosphate groups surrounded by polar amino acids and the carbons are surrounded by non-polar amino acids which makes it favorable for the ligand and active site. PLP has polar (hydrophilic) portions that are exposed to the surrounding and non-polar (hydophobic) protions that are hidden within the protein making it stable. Hydrogen bonding and pi-stacking stabilize the <scene name='94/941534/Ligand_of_interest/1'>ligand</scene> and the active site.
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/>

Sandbox Reserved 1763&action=edit

2022-12-13T18:28:01Z

Carmen J Almendarez Rodriguez:

==Human Orthinine Aminotransferase (hOAT)==
<StructureSection load='7t9z' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Sandbox Reserved 1763&action=edit'''. 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 Orthinine Aminotransferase (OAT) and hOAT in humans is an enzyme that catalyzes the transfer of an amino acid group L-orthinine from L-orthinine to an alpha-ketoglutarate. Its ligand pyrodixal-5-phosphate (PLP) is a cofactor in the reaction. An amino group from L-orthinine is transferred to PLP which converts it to pyridoxamine phosphate (PMP) and L-orthinine is converted to L-glutamate-y-semialdehyde. PLP is regenerated when PMP is transferred to alpha-KG.
== Bilogical relavance and broader implications ==
hOAT is an enzyme that is found in almost all tissues but predominately in the liver and kidney. There is an overexpression of hOAT in cancer cells so understanding it can help the proliferation of cancer cells, especially hepatocellular carcinoma (HCC) which is a type of liver cell. hOAT has been a target mechanism-based inactivator (MBIs) in an attempt to create drugs. HCC is generally diagnosed in advanced stages which makes cancer more resistant to chemotherapy. hOAT inhibitors were created as fragmented-sized alternative substrates such as y-aminobutyric acid (GABA) and 5-aminovaleric acid (AVA). GABA is covalently bonded to PLP. While AVA is covalently attached to PLP by lysine 292, which is a catalytic enzyme in the binding pocket. GABA and AVA have strong binding affinity but slow turnovers.
== Important amino acids ==
The amino acids in the PLP binding site are <scene name='94/941534/Lysine_292/1'>Lys 292</scene>, Asp 263, Arg 180, and Phe 177. They are essential in the active site because of their interaction with PLP. PLP is covalently bonded to the amino acid lysine. The nitrogen in the ring of PLP interacts with the negatively charged oxygen in the aspartate side chain. The phosphate interacts with the positively charged nitrogen of the arginine side chain. And Phe 177 has a pi- stacking interaction between its ring and the ring of PLP
== Structural highlights ==
hOAT is a protein with a secondary structure that is mainly made of alpha helices but also has parallel and anti-parallel beta sheets and random coil. Its a polymer with a globular structure that has three subunits held by non-cavantly interactions like hydrogen bond and salt bridges between the side chains and amino acids. The binding pocket is semi-exposed which makes helps competitive substrates bind to the active site. The PLP has a phosphate groups surrounded by polar amino acids and the carbons are surrounded by non-polar amino acids which makes it favorable for the ligand and active site. PLP has polar (hydrophilic) portions that are exposed to the surrounding and non-polar (hydophobic) protions that are hidden within the protein making it stable. Hydrogen bonding and pi-stacking stabilize the <scene name='94/941534/Ligand_of_interest/1'>ligand</scene> and the active site.
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/>

Sandbox Reserved 1763&action=edit

2022-12-13T18:15:51Z

Carmen J Almendarez Rodriguez:

==Human Orthinine Aminotransferase (hOAT)==
<StructureSection load='7t9z' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Sandbox Reserved 1763&action=edit'''. 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 Orthinine Aminotransferase (OAT) and hOAT in humans is an enzyme that catalyzes the transfer of an amino acid group L-orthinine from L-orthinine to an alpha-ketoglutarate. Its ligand pyrodixal-5-phosphate (PLP) is a cofactor in the reaction. An amino group from L-orthinine is transferred to PLP which converts it to pyridoxamine phosphate (PMP) and L-orthinine is converted to L-glutamate-y-semialdehyde. PLP is regenerated when PMP is transferred to alpha-KG.
== Bilogical relavance and broader implications ==
hOAT is an enzyme that is found in almost all tissues but predominately in the liver and kidney. There is an overexpression of hOAT in cancer cells so understanding it can help the proliferation of cancer cells, especially hepatocellular carcinoma (HCC) which is a type of liver cell. hOAT has been a target mechanism-based inactivator (MBIs) in an attempt to create drugs. HCC is generally diagnosed in advanced stages which makes cancer more resistant to chemotherapy. hOAT inhibitors were created as fragmented-sized alternative substrates such as y-aminobutyric acid (GABA) and 5-aminovaleric acid (AVA). GABA is covalently bonded to PLP. While AVA is covalently attached to PLP by lysine 292, which is a catalytic enzyme in the binding pocket. GABA and AVA have strong binding affinity but slow turnovers.
== Important amino acids ==
The amino acids in the PLP binding site are Lys 292, Asp 263, Arg 180, and Phe 177. They are essential in the active site because of their interaction with PLP. PLP is covalently bonded to the amino acid lysine. The nitrogen in the ring of PLP interacts with the negatively charged oxygen in the aspartate side chain. The phosphate interacts with the positively charged nitrogen of the arginine side chain. And Phe 177 has a pi- stacking interaction between its ring and the ring of PLP
== Structural highlights ==
hOAT is a protein with a secondary structure that is mainly made of alpha helices but also has parallel and anti-parallel beta sheets and random coil. Its a polymer with a globular structure that has three subunits held by non-cavantly interactions like hydrogen bond and salt bridges between the side chains and amino acids. The binding pocket is semi-exposed which makes helps competitive substrates bind to the active site. The PLP has a phosphate groups surrounded by polar amino acids and the carbons are surrounded by non-polar amino acids which makes it favorable for the ligand and active site. PLP has polar (hydrophilic) portions that are exposed to the surrounding and non-polar (hydophobic) protions that are hidden within the protein making it stable. Hydrogen bonding and pi-stacking stabilize the <scene name='94/941534/Ligand_of_interest/1'>ligand</scene> and the active site.
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/>

Sandbox Reserved 1763&action=edit

2022-12-13T18:12:02Z

Carmen J Almendarez Rodriguez:

==Human Orthinine Aminotransferase (hOAT)==
<StructureSection load='7t9z' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Sandbox Reserved 1763&action=edit'''. 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 Orthinine Aminotransferase (OAT) and hOAT in humans is an enzyme that catalyzes the transfer of an amino acid group L-orthinine from L-orthinine to an alpha-ketoglutarate. Its ligand pyrodixal-5-phosphate (PLP) is a cofactor in the reaction. An amino group from L-orthinine is transferred to PLP which converts it to pyridoxamine phosphate (PMP) and L-orthinine is converted to L-glutamate-y-semialdehyde. PLP is regenerated when PMP is transferred to alpha-KG.
== Bilogical relavance and broader implications ==
hOAT is an enzyme that is found in almost all tissues but predominately in the liver and kidney. There is an overexpression of hOAT in cancer cells so understanding it can help the proliferation of cancer cells, especially hepatocellular carcinoma (HCC) which is a type of liver cell. hOAT has been a target mechanism-based inactivator (MBIs) in an attempt to create drugs. HCC is generally diagnosed in advanced stages which makes cancer more resistant to chemotherapy. hOAT inhibitors were created as fragmented-sized alternative substrates such as y-aminobutyric acid (GABA) and 5-aminovaleric acid (AVA). GABA is covalently bonded to PLP. While AVA is covalently attached to PLP by lysine 292, which is a catalytic enzyme in the binding pocket. GABA and AVA have strong binding affinity but slow turnovers.
== Important amino acids ==
The amino acids in the PLP binding site are Lys 292, Asp 263, Arg 180, and Phe 177. They are essential in the active site because of their interaction with PLP. PLP is covalently bonded to the amino acid lysine. The nitrogen in the ring of PLP interacts with the negatively charged oxygen in the aspartate side chain. The phosphate interacts with the positively charged nitrogen of the arginine side chain. And Phe 177 has a pi- stacking interaction between its ring and the ring of PLP
== Structural highlights ==
hOAT is a protein with a secondary structure that is mainly made of alpha helices but also has parallel and anti-parallel beta sheets and random coil. Its a polymer with a globular structure that has three subunits held by non-cavantly interactions like hydrogen bond and salt bridges between the side chains and amino acids. The binding pocket is semi-exposed which makes helps competitive substrates bind to the active site. The PLP has a phosphate groups surrounded by polar amino acids and the carbons are surrounded by non-polar amino acids which makes it favorable for the ligand and active site. PLP has polar (hydrophilic) portions that are exposed to the surrounding and non-polar (hydophobic) protions that are hidden within the protein making it stable. Hydrogen bonding and pi-stacking stabilize the ligand and the active site.
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/>

Sandbox Reserved 1763&action=edit

2022-12-13T18:11:04Z

Carmen J Almendarez Rodriguez:

==Your Heading Here (maybe something like 'Structure')==
<StructureSection load='7t9z' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Sandbox Reserved 1763&action=edit'''. 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 Orthinine Aminotransferase (OAT) and hOAT in humans is an enzyme that catalyzes the transfer of an amino acid group L-orthinine from L-orthinine to an alpha-ketoglutarate. Its ligand pyrodixal-5-phosphate (PLP) is a cofactor in the reaction. An amino group from L-orthinine is transferred to PLP which converts it to pyridoxamine phosphate (PMP) and L-orthinine is converted to L-glutamate-y-semialdehyde. PLP is regenerated when PMP is transferred to alpha-KG.
== Bilogical relavance and broader implications ==
hOAT is an enzyme that is found in almost all tissues but predominately in the liver and kidney. There is an overexpression of hOAT in cancer cells so understanding it can help the proliferation of cancer cells, especially hepatocellular carcinoma (HCC) which is a type of liver cell. hOAT has been a target mechanism-based inactivator (MBIs) in an attempt to create drugs. HCC is generally diagnosed in advanced stages which makes cancer more resistant to chemotherapy. hOAT inhibitors were created as fragmented-sized alternative substrates such as y-aminobutyric acid (GABA) and 5-aminovaleric acid (AVA). GABA is covalently bonded to PLP. While AVA is covalently attached to PLP by lysine 292, which is a catalytic enzyme in the binding pocket. GABA and AVA have strong binding affinity but slow turnovers.
== Important amino acids ==
The amino acids in the PLP binding site are Lys 292, Asp 263, Arg 180, and Phe 177. They are essential in the active site because of their interaction with PLP. PLP is covalently bonded to the amino acid lysine. The nitrogen in the ring of PLP interacts with the negatively charged oxygen in the aspartate side chain. The phosphate interacts with the positively charged nitrogen of the arginine side chain. And Phe 177 has a pi- stacking interaction between its ring and the ring of PLP
== Structural highlights ==
hOAT is a protein with a secondary structure that is mainly made of alpha helices but also has parallel and anti-parallel beta sheets and random coil. Its a polymer with a globular structure that has three subunits held by non-cavantly interactions like hydrogen bond and salt bridges between the side chains and amino acids. The binding pocket is semi-exposed which makes helps competitive substrates bind to the active site. The PLP has a phosphate groups surrounded by polar amino acids and the carbons are surrounded by non-polar amino acids which makes it favorable for the ligand and active site. PLP has polar (hydrophilic) portions that are exposed to the surrounding and non-polar (hydophobic) protions that are hidden within the protein making it stable. Hydrogen bonding and pi-stacking stabilize the ligand and the active site.
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/>

Sandbox Reserved 1763&action=edit

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Carmen J Almendarez Rodriguez:

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2022-12-13T17:30:53Z

Carmen J Almendarez Rodriguez: New page: ==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 you...

==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 '''Sandbox Reserved 1763&action=edit'''. 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/>

Sandbox Reserved 1763

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Carmen J Almendarez Rodriguez:

{{Sandbox_Reserved_BHall_F22}}
==Human Ornithinine Aminotransferase (hOAT)==
<StructureSection load='7T9Z' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page ''''''. 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 of your protein ==
The protein Ornithinine Aminotransferase (OAT), in humans (hOAT), is an enzyme that catalyzes the reaction between carbamoyl phosphate and orthinine to form citrulline and phosphate. Its ligand is pyridoxal-5'phosphate (PLP) which is a cofactor of the reaction. An amino group from L-Orn is transferred to PLP which turns it into pyridoxine phosphate (PMP) and L-Orn is converted to L glutamate-y-semialdehyde. PLP is regenerated when the amino group PMP is transferred to alpha-KG. It has 3 ligands pyridoxal-5' phosphate (PLP) which is a cofactor in the reaction. An amino group from L-Ornithinine is transferred to PLP which converts it to pyridoxamine phosphate (PMP) and L-Orn is converted to L-glutamate-y-semialdehyde. PLP is regenerated when PMP is transferred to alpha-KG.

== Biological relevance and broader implications ==
hOAT is a ubiquitous enzyme found in almost all organisms and has been found to be overexpressed in hepatocellular carcinoma cells (HCC), which is a type of liver cancer. It is found predominantly in the liver and kidney. The liver, where it is an integral part of the urea cycle, and the intestine, where it synthesizes citrulline for export and plays a major role in amino acid homeostasis, particularly of L-glutamine and L-arginine. Studying this protein could be a potential drug to target cancer as a different therapy and radiation. hOAT has been a target mechanism-based inactivator (MBIs) in drug design efforts. HCC has diagnosed an advanced type of cancer which makes it more resistant to chemotherapy. hOAT inhibitors were created as fragmented-sized alternative substances such as GABA and 5-aminovaleric acid (AVA). hOAT was soaked with GABA and AVA and the new substrates prevented original interactions with catalytic amino acids and the ligand (PLP) which creates a tighter to hOAT instead of L-ornithine. GABA and AVA had a stronger binding affinity and slower turnovers which makes them potential drug targets for hOAT.

== Important amino acids==
Amino Acids in PLP binding site are ,Lys 292</scene> Asp 263, Phe 177 and Arg 180</scene>.<ref> 35460691 </ref>. They are essential to the active site. PLP is covalently bonded to the amino acid lysine. The phosphate group interacts with the positively charged nitrogen of the arginine side chain. There is also a pi-stacking interaction between its ring and the ring of PLP.

== Structural highlights ==
hOAT is a protein with a <scene name='93/934007/Secondary_structure/1'>secondary structure</scene> consisting of mainly alpha-helices but it also has parallel and anti-parallel beta-sheets and random coil. It's a polymer with a <scene name='93/934007/Globular_module/1'>globular structure</scene> that has three subunits held together by non-covalent interactions such as hydrogen bonds and salt bridges hidden in the protein. The <scene name='93/934007/Ligands_of_interest/1'>ligand</scene> has a phosphate group surrounded by polar amino acids, and carbons are surrounded by non-polar amino acids to satisfy the needs of the ligand and active site. Interactions like hydrogen bonding and pi-stacking stabilize and bind the ligand in the active site. The binding pocket of PLP is semi-exposed to the surrounding. The binding pockets can help competitive substrates to bind to the active site and inhibit the enzyme. The PLP ligand has a phosphate group that is surrounded by other polar amino acids and the carbons are surrounded by other non-polar acids which makes it favorable for the ligand and active site. The polar (hydrophilic) portions of the would-be unstable if they tried to interact with the non-polar (hydrophobic) surrounding. Interactions like hydrogen bonding and pi-stacking stabilize and bind the ligand to the active site.
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/>

Sandbox Reserved 1763

2022-12-13T16:27:20Z

Carmen J Almendarez Rodriguez:

{{Sandbox_Reserved_BHall_F22}}
==Human Ornithinine Aminotransferase (hOAT)==
<StructureSection load='7T9Z' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page ''''''. 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 of your protein ==
The protein Ornithinine Aminotransferase (OAT), in humans (hOAT), is an enzyme that catalyzes the reaction between carbamoyl phosphate and orthinine to form citrulline and phosphate. Its ligand is pyridoxal-5'phosphate (PLP) which is a cofactor of the reaction. An amino group from L-Orn is transferred to PLP which turns it into pyridoxine phosphate (PMP) and L-Orn is converted to L glutamate-y-semialdehyde. PLP is regenerated when the amino group PMP is transferred to alpha-KG.

== Biological relevance and broader implications ==
hOAT is a ubiquitous enzyme found in almost all organisms and has been found to be overexpressed in hepatocellular carcinoma cells (HCC), which is a type of liver cancer. It is found predominantly in the liver and kidney. The liver, where it is an integral part of the urea cycle, and the intestine, where it synthesizes citrulline for export and plays a major role in amino acid homeostasis, particularly of L-glutamine and L-arginine. Studying this protein could be a potential drug to target cancer as a different therapy and radiation. hOAT has been a target mechanism-based inactivator (MBIs) in drug design efforts. HCC has diagnosed an advanced type of cancer which makes it more resistant to chemotherapy. hOAT inhibitors were created as fragmented-sized alternative substances such as GABA and 5-aminovaleric acid (AVA). hOAT was soaked with GABA and AVA and the new substrates prevented original interactions with catalytic amino acids and the ligand (PLP) which creates a tighter to hOAT instead of L-ornithine. GABA and AVA had a stronger binding affinity and slower turnovers which makes them potential drug targets for hOAT.

== Important amino acids==
Amino Acids in PLP binding site are <scene name='93/934007/Amino_acids/2'><scene name='93/934007/Lysine_292/1'>Lys 292</scene>, Asp 263, Phe 177 and Arg 180</scene>. <ref> 35460691 </ref>. They are essential to the active site. PLP is covalently bonded to the amino acid lysine. The phosphate group interacts with the positively charged nitrogen of the arginine side chain. There is also a pi-stacking interaction between its ring and the ring of PLP.
== Structural highlights ==
hOAT is a protein with a <scene name='93/934007/Secondary_structure/1'>secondary structure</scene> consisting of mainly alpha-helices but it also has parallel and anti-parallel beta-sheets and random coil. It's a polymer with a <scene name='93/934007/Globular_module/1'>globular structure</scene> that has three subunits held together by non-covalent interactions such as hydrogen bonds and salt bridges hidden in the protein. The <scene name='93/934007/Ligands_of_interest/1'>ligand</scene> has a phosphate group surrounded by polar amino acids, and carbons are surrounded by non-polar amino acids to satisfy the needs of the ligand and active site. Interactions like hydrogen bonding and pi-stacking stabilize and bind the ligand in the active site.
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/>

Sandbox Reserved 1763

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Carmen J Almendarez Rodriguez:

{{Sandbox_Reserved_BHall_F22}}
==Human Ornithinine Aminotransferase (hOAT)==
<StructureSection load='7T9Z' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page ''''''. 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 of your protein ==
The protein Ornithinine Aminotransferase (OAT), in humans (hOAT), is an enzyme that catalyzes the reaction between carbamoyl phosphate and orthinine to form citrulline and phosphate. Its ligand is pyridoxal-5'phosphate (PLP) which is a cofactor of the reaction. An amino group from L-Orn is transferred to PLP which turns it into pyridoxine phosphate (PMP) and L-Orn is converted to L glutamate-y-semialdehyde. PLP is regenerated when the amino group PMP is transferred to alpha-KG.

== Biological relevance and broader implications ==
hOAT is a ubiquitous enzyme found in almost all organisms and has been found to be overexpressed in hepatocellular carcinoma cells (HCC), which is a type of liver cancer. It is found predominantly in the liver and kidney. The liver, where it is an integral part of the urea cycle, and the intestine, where it synthesizes citrulline for export and plays a major role in amino acid homeostasis, particularly of L-glutamine and L-arginine. Studying this protein could be a potential drug to target cancer as a different therapy and radiation. hOAT has been a target mechanism-based inactivator (MBIs) in drug design efforts. HCC has diagnosed an advanced type of cancer which makes it more resistant to chemotherapy. hOAT inhibitors were created as fragmented-sized alternative substances such as GABA and 5-aminovaleric acid (AVA). hOAT was soaked with GABA and AVA and the new substrates prevented original interactions with catalytic amino acids and the ligand (PLP) which creates a tighter to hOAT instead of L-ornithine. GABA and AVA had a stronger binding affinity and slower turnovers which makes them potential drug targets for hOAT.

== Important amino acids==
Amino Acids in PLP binding site are <scene name='93/934007/Amino_acids/2'>Lys 292, Asp 263, Phe 177 and Arg 180</scene>. <ref> 35460691 </ref>. They are essential to the active site. PLP is covalently bonded to the amino acid lysine. The phosphate group interacts with the positively charged nitrogen of the arginine side chain. There is also a pi-stacking interaction between its ring and the ring of PLP.
== Structural highlights ==
hOAT is a protein with a <scene name='93/934007/Secondary_structure/1'>secondary structure</scene> consisting of mainly alpha-helices but it also has parallel and anti-parallel beta-sheets and random coil. It's a polymer with a <scene name='93/934007/Globular_module/1'>globular structure</scene> that has three subunits held together by non-covalent interactions such as hydrogen bonds and salt bridges hidden in the protein. The <scene name='93/934007/Ligands_of_interest/1'>ligand</scene> has a phosphate group surrounded by polar amino acids, and carbons are surrounded by non-polar amino acids to satisfy the needs of the ligand and active site. Interactions like hydrogen bonding and pi-stacking stabilize and bind the ligand in the active site.
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/>

Sandbox Reserved 1763

2022-12-13T02:41:42Z

Carmen J Almendarez Rodriguez:

{{Sandbox_Reserved_BHall_F22}}
==Human Ornithinine Aminotransferase (hOAT)==
<StructureSection load='7T9Z' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page ''''''. 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 of your protein ==
The protein Ornithinine Aminotransferase (OAT), in humans (hOAT), is an enzyme that catalyzes the reaction between carbamoyl phosphate and orthinine to form citrulline and phosphate. Its ligand is pyridoxal-5'phosphate (PLP) which is a cofactor of the reaction. An amino group from L-Orn is transferred to PLP which turns it into pyridoxine phosphate (PMP) and L-Orn is converted to L glutamate-y-semialdehyde. PLP is regenerated when the amino group PMP is transferred to alpha-KG.

== Biological relevance and broader implications ==
hOAT is a ubiquitous enzyme found in almost all organisms and has been found to be overexpressed in hepatocellular carcinoma cells (HCC), which is a type of liver cancer. It is found predominantly in the liver and kidney. The liver, where it is an integral part of the urea cycle, and the intestine, where it synthesizes citrulline for export and plays a major role in amino acid homeostasis, particularly of L-glutamine and L-arginine. Studying this protein could be a potential drug to target cancer as a different therapy and radiation. hOAT has been a target mechanism-based inactivator (MBIs) in drug design efforts. HCC has diagnosed an advanced type of cancer which makes it more resistant to chemotherapy. hOAT inhibitors were created as fragmented-sized alternative substances such as GABA and 5-aminovaleric acid (AVA). hOAT was soaked with GABA and AVA and the new substrates prevented original interactions with catalytic amino acids and the ligand (PLP) which creates a tighter to hOAT instead of L-ornithine. GABA and AVA had a stronger binding affinity and slower turnovers which makes them potential drug targets for hOAT.

== Important amino acids==
Amino Acids in PLP binding site are <scene name='93/934007/Amino_acids/2'>Lys 292, Asp 263, Phe 177 and Arg 180</scene>. <ref> 35460691 </ref>. They are essential to the active site. PLP is covalently bonded to the amino acid lysine. The phosphate group interacts with the positively charged nitrogen of the arginine side chain. There is also a pi-stacking interaction between its ring and the ring of PLP.
== Structural highlights ==
hOAT is a protein with a <scene name='93/934007/Secondary_structure/1'>secondary structure</scene> consisting of mainly alpha-helices but it also has parallel and anti-parallel beta-sheets and random coil. It's a polymer with a globular structure that has three subunits held together by non-covalent interactions such as hydrogen bonds and salt bridges hidden in the protein. The <scene name='93/934007/Ligands_of_interest/1'>ligand</scene> has a phosphate group surrounded by polar amino acids, and carbons are surrounded by non-polar amino acids to satisfy the needs of the ligand and active site. Interactions like hydrogen bonding and pi-stacking stabilize and bind the ligand in the active site.
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/>

Sandbox Reserved 1763

2022-12-13T02:32:21Z

Carmen J Almendarez Rodriguez:

{{Sandbox_Reserved_BHall_F22}}
==Human Ornithinine Aminotransferase (hOAT)==
<StructureSection load='7T9Z' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page ''''''. 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 of your protein ==
The protein Ornithinine Aminotransferase (OAT), in humans (hOAT), is an enzyme that catalyzes the reaction between carbamoyl phosphate and orthinine to form citrulline and phosphate. Its ligand is pyridoxal-5'phosphate (PLP) which is a cofactor of the reaction. An amino group from L-Orn is transferred to PLP which turns it into pyridoxine phosphate (PMP) and L-Orn is converted to L glutamate-y-semialdehyde. PLP is regenerated when the amino group PMP is transferred to alpha-KG.

== Biological relevance and broader implications ==
hOAT is a ubiquitous enzyme found in almost all organisms and has been found to be overexpressed in hepatocellular carcinoma cells (HCC), which is a type of liver cancer. It is found predominantly in the liver and kidney. The liver, where it is an integral part of the urea cycle, and the intestine, where it synthesizes citrulline for export and plays a major role in amino acid homeostasis, particularly of L-glutamine and L-arginine. Studying this protein could be a potential drug to target cancer as a different therapy and radiation. hOAT has been a target mechanism-based inactivator (MBIs) in drug design efforts. HCC has diagnosed an advanced type of cancer which makes it more resistant to chemotherapy. hOAT inhibitors were created as fragmented-sized alternative substances such as GABA and 5-aminovaleric acid (AVA). hOAT was soaked with GABA and AVA and the new substrates prevented original interactions with catalytic amino acids and the ligand (PLP) which creates a tighter to hOAT instead of L-ornithine. GABA and AVA had a stronger binding affinity and slower turnovers which makes them potential drug targets for hOAT.

== Important amino acids==
Amino Acids in PLP binding site are <scene name='93/934007/Amino_acids/2'>Lys 292, Asp 263, Phe 177 and Arg 180</scene>. <ref> 35460691 </ref>. They are essential to the active site. PLP is covalently bonded to the amino acid lysine. The phosphate group interacts with the positively charged nitrogen of the arginine side chain. There is also a pi-stacking interaction between its ring and the ring of PLP.
== Structural highlights ==
hOAT is a protein with a secondary structure consisting of mainly alpha-helices but it also has parallel and anti-parallel beta-sheets and random coil. It's a polymer with a globular structure that has three subunits held together by non-covalent interactions such as hydrogen bonds and salt bridges hidden in the protein. The <scene name='93/934007/Ligands_of_interest/1'>ligand</scene> has a phosphate group surrounded by polar amino acids, and carbons are surrounded by non-polar amino acids to satisfy the needs of the ligand and active site. Interactions like hydrogen bonding and pi-stacking stabilize and bind the ligand in the active site.
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/>

Sandbox Reserved 1763

2022-12-13T02:20:39Z

Carmen J Almendarez Rodriguez:

{{Sandbox_Reserved_BHall_F22}}
==Human Ornithinine Aminotransferase (hOAT)==
<StructureSection load='7T9Z' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page ''''''. 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 of your protein ==
The protein Ornithinine Aminotransferase (OAT), in humans (hOAT), is an enzyme that catalyzes the reaction between carbamoyl phosphate and orthinine to form citrulline and phosphate. Its ligand is pyridoxal-5'phosphate (PLP) which is a cofactor of the reaction. An amino group from L-Orn is transferred to PLP which turns it into pyridoxine phosphate (PMP) and L-Orn is converted to L glutamate-y-semialdehyde. PLP is regenerated when the amino group PMP is transferred to alpha-KG.

== Biological relevance and broader implications ==
hOAT is a ubiquitous enzyme found in almost all organisms and has been found to be overexpressed in hepatocellular carcinoma cells (HCC), which is a type of liver cancer. It is found predominantly in the liver and kidney. The liver, where it is an integral part of the urea cycle, and the intestine, where it synthesizes citrulline for export and plays a major role in amino acid homeostasis, particularly of L-glutamine and L-arginine. Studying this protein could be a potential drug to target cancer as a different therapy and radiation. hOAT has been a target mechanism-based inactivator (MBIs) in drug design efforts. HCC has diagnosed an advanced type of cancer which makes it more resistant to chemotherapy. hOAT inhibitors were created as fragmented-sized alternative substances such as GABA and 5-aminovaleric acid (AVA). hOAT was soaked with GABA and AVA and the new substrates prevented original interactions with catalytic amino acids and the ligand (PLP) which creates a tighter to hOAT instead of L-ornithine. GABA and AVA had a stronger binding affinity and slower turnovers which makes them potential drug targets for hOAT.

== Important amino acids==
Amino Acids in PLP binding site are <scene name='93/934007/Amino_acids/2'>Lys 292, Asp 263, Phe 177 and Arg 180</scene>. They are essential to the active site. PLP is covalently bonded to the amino acid lysine. The phosphate group interacts with the positively charged nitrogen of the arginine side chain. There is also a pi-stacking interaction between its ring and the ring of PLP.
== Structural highlights ==
hOAT is a protein with a secondary structure consisting of mainly alpha-helices but it also has parallel and anti-parallel beta-sheets and random coil. It's a polymer with a globular structure that has three subunits held together by non-covalent interactions such as hydrogen bonds and salt bridges hidden in the protein. The <scene name='93/934007/Ligands_of_interest/1'>ligand</scene> has a phosphate group surrounded by polar amino acids, and carbons are surrounded by non-polar amino acids to satisfy the needs of the ligand and active site. Interactions like hydrogen bonding and pi-stacking stabilize and bind the ligand in the active site.
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/>

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{{Sandbox_Reserved_BHall_F22}}
==Human Ornithinine Aminotransferase (hOAT)==
<StructureSection load='7T9Z' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page ''''''. 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 of your protein ==
The protein Ornithinine Aminotransferase (OAT), in humans (hOAT), is an enzyme that catalyzes the reaction between carbamoyl phosphate and orthinine to form citrulline and phosphate. Its ligand is pyridoxal-5'phosphate (PLP) which is a cofactor of the reaction. An amino group from L-Orn is transferred to PLP which turns it into pyridoxine phosphate (PMP) and L-Orn is converted to L glutamate-y-semialdehyde. PLP is regenerated when the amino group PMP is transferred to alpha-KG.

== Biological relevance and broader implications ==
hOAT is a ubiquitous enzyme found in almost all organisms and has been found to be overexpressed in hepatocellular carcinoma cells (HCC), which is a type of liver cancer. It is found predominantly in the liver and kidney. The liver, where it is an integral part of the urea cycle, and the intestine, where it synthesizes citrulline for export and plays a major role in amino acid homeostasis, particularly of L-glutamine and L-arginine. Studying this protein could be a potential drug to target cancer as a different therapy and radiation. hOAT has been a target mechanism-based inactivator (MBIs) in drug design efforts. HCC has diagnosed an advanced type of cancer which makes it more resistant to chemotherapy. hOAT inhibitors were created as fragmented-sized alternative substances such as GABA and 5-aminovaleric acid (AVA). hOAT was soaked with GABA and AVA and the new substrates prevented original interactions with catalytic amino acids and the ligand (PLP) which creates a tighter to hOAT instead of L-ornithine. GABA and AVA had a stronger binding affinity and slower turnovers which makes them potential drug targets for hOAT.

== Important amino acids==
Amino Acids in PLP binding site are Lys 292, Asp 263, and Arg 180. They are essential to the active site. PLP is covalently bonded to the amino acid lysine. The phosphate group interacts with the positively charged nitrogen of the arginine side chain. There is also a pi-stacking interaction between its ring and the ring of PLP.
== Structural highlights ==
hOAT is a protein with a secondary structure consisting of mainly alpha-helices but it also has parallel and anti-parallel beta-sheets and random coil. It's a polymer with a globular structure that has three subunits held together by non-covalent interactions such as hydrogen bonds and salt bridges hidden in the protein. The <scene name='93/934007/Ligands_of_interest/1'>ligand</scene> has a phosphate group surrounded by polar amino acids, and carbons are surrounded by non-polar amino acids to satisfy the needs of the ligand and active site. Interactions like hydrogen bonding and pi-stacking stabilize and bind the ligand in the active site.
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/>

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Carmen J Almendarez Rodriguez:

{{Sandbox_Reserved_BHall_F22}}
==Your Heading Here (hOAT)==
<StructureSection load='7T9Z' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page ''''''. 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 of your protein ==
The protein Ornithinine Aminotransferase (OAT), in humans (hOAT), is an enzyme that catalyzes the reaction between carbamoyl phosphate and orthinine to form citrulline and phosphate. Its ligand is pyridoxal-5'phosphate (PLP) which is a cofactor of the reaction. An amino group from L-Orn is transferred to PLP which turns it into pyridoxine phosphate (PMP) and L-Orn is converted to L glutamate-y-semialdehyde. PLP is regenerated when the amino group PMP is transferred to alpha-KG.

== Biological relevance and broader implications ==
hOAT is a ubiquitous enzyme found in almost all organisms and has been found to be overexpressed in hepatocellular carcinoma cells (HCC), which is a type of liver cancer. It is found predominantly in the liver and kidney. The liver, where it is an integral part of the urea cycle, and the intestine, where it synthesizes citrulline for export and plays a major role in amino acid homeostasis, particularly of L-glutamine and L-arginine. Studying this protein could be a potential drug to target cancer as a different therapy and radiation. hOAT has been a target mechanism-based inactivator (MBIs) in drug design efforts. HCC has diagnosed an advanced type of cancer which makes it more resistant to chemotherapy. hOAT inhibitors were created as fragmented-sized alternative substances such as GABA and 5-aminovaleric acid (AVA). hOAT was soaked with GABA and AVA and the new substrates prevented original interactions with catalytic amino acids and the ligand (PLP) which creates a tighter to hOAT instead of L-ornithine. GABA and AVA had a stronger binding affinity and slower turnovers which makes them potential drug targets for hOAT.

== Important amino acids==
Amino Acids in PLP binding site are Lys 292, Asp 263, and Arg 180. They are essential to the active site. PLP is covalently bonded to the amino acid lysine. The phosphate group interacts with the positively charged nitrogen of the arginine side chain. There is also a pi-stacking interaction between its ring and the ring of PLP.
== Structural highlights ==
hOAT is a protein with a secondary structure consisting of mainly alpha-helices but it also has parallel and anti-parallel beta-sheets and random coil. It's a polymer with a globular structure that has three subunits held together by non-covalent interactions such as hydrogen bonds and salt bridges hidden in the protein. The <scene name='93/934007/Ligands_of_interest/1'>ligand</scene> has a phosphate group surrounded by polar amino acids, and carbons are surrounded by non-polar amino acids to satisfy the needs of the ligand and active site. Interactions like hydrogen bonding and pi-stacking stabilize and bind the ligand in the active site.
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/>

Sandbox Reserved 1763

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Carmen J Almendarez Rodriguez:

{{Sandbox_Reserved_BHall_F22}}
==Your Heading Here (maybe something like 'Structure')==
<StructureSection load='7T9Z' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page ''''''. 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 of your protein ==
The protein Ornithinine Aminotransferase (OAT), in humans (hOAT), is an enzyme that catalyzes the reaction between carbamoyl phosphate and orthinine to form citrulline and phosphate. Its ligand is pyridoxal-5'phosphate (PLP) which is a cofactor of the reaction. An amino group from L-Orn is transferred to PLP which turns it into pyridoxine phosphate (PMP) and L-Orn is converted to L glutamate-y-semialdehyde. PLP is regenerated when the amino group PMP is transferred to alpha-KG.

== Biological relevance and broader implications ==
hOAT is an ubiquitous enzyme found in almost all organisms has been found to be overexpressed in hepatocellular carcinoma cells (HCC), which is a type of liver cancer. It is found predominantly in the liver and kidney. The liver, where it is an integral part of the urea cycle, and the intestine, where it synthesizes citrulline for export and plays a major role in amino acid homeostasis, particularly of L-glutamine and L-arginine.Studying this protein could be a potential drug to target cancer as a different therapy and radiation. hOAT has been a target mechanism-based inactivator (MBIs) in drug design efforts. HCC is diagnosed in advanced type of cancer which makes it more resistant to chemotherapy. hOAT inhibitors were created as fragmented-sized alternative substances such as GABA and 5-aminovaleric acid (AVA). hOAT was soaked with GABA and AVA and the new substrates prevented original interactions with catalytic amino acids and the ligand (PLP) which creates a tighter to hOAT instead of L-ornithine. GABA and AVA had stronger binding affinity and slower turnovers which makes them potential drug targets for hOAT.

== Important amino acids==
Amino Acids in PLP binding site are Lys 292, Asp 263, and Arg 180. They are essential to the active site. PLP is covalently bonded to the amino acid lysine. The phosphate group interacts with the positively charged nitrogen of the arginine side chain. There is also a pi-stacking interaction between its ring and the ring of PLP.
== Structural highlights ==
hOAT is a protein with a secondary structure consisting of mainly alpha-helices but it also has parallel and anti-parallel beta-sheets and random coil. It's a polymer with a globular structure that has three subunits held together by non-covalent interactions such as hydrogen bonds and salt bridges hidden in the protein. The <scene name='93/934007/Ligands_of_interest/1'>ligand</scene> has a phosphate group surrounded by polar amino acids, carbons are surrounded by non-polar amino acids to satisfy the needs of the ligand and active site. Interactions like hydrogen bonding and pi-stacking stabilize and bind the ligand in the active site.
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/>

Sandbox Reserved 1763

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Carmen J Almendarez Rodriguez:

{{Sandbox_Reserved_BHall_F22}}
==Your Heading Here (maybe something like 'Structure')==
<StructureSection load='7T9Z' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page ''''''. 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 of your protein ==
The protein Ornithinine Aminotransferase (OAT), in humans (hOAT), is an enzyme that catalyzes the reaction between carbamoyl phosphate and orthinine to form citrulline and phosphate. Its ligand is pyridoxal-5'phosphate (PLP) which is a cofactor of the reaction. An amino group from L-Orn is transferred to PLP which turns it into pyridoxine phosphate (PMP) and L-Orn is converted to L glutamate-y-semialdehyde. PLP is regenerated when the amino group PMP is transferred to alpha-KG.

== Biological relevance and broader implications ==
hOAT is an ubiquitous enzyme found in almost all organisms has been found to be overexpressed in hepatocellular carcinoma cells (HCC), which is a type of liver cancer. It is found predominantly in the liver and kidney. The liver, where it is an integral part of the urea cycle, and the intestine, where it synthesizes citrulline for export and plays a major role in amino acid homeostasis, particularly of L-glutamine and L-arginine.Studying this protein could be a potential drug to target cancer as a different therapy and radiation. hOAT has been a target mechanism-based inactivator (MBIs) in drug design efforts. HCC is diagnosed in advanced type of cancer which makes it more resistant to chemotherapy. hOAT inhibitors were created as fragmented-sized alternative substances such as GABA and 5-aminovaleric acid (AVA). hOAT was soaked with GABA and AVA and the new substrates prevented original interactions with catalytic amino acids and the ligand (PLP) which creates a tighter to hOAT instead of L-ornithine. GABA and AVA had stronger binding affinity and slower turnovers which makes them potential drug targets for hOAT.

== Important amino acids==
Amino Acids in PLP binding site are Lys 292, Asp 263, and Arg 180. They are essential to the active site. PLP is covalently bonded to the amino acid lysine. The phosphate group interacts with the positively charged nitrogen of the arginine side chain. There is also a pi-stacking interaction between its ring and the ring of PLP.
== Structural highlights ==
hOAT is a protein with a secondary structure consisting of mainly alpha-helices but it also has parallel and anti-parallel beta-sheets and random coil. It's a polymer with a globular structure that has three subunits held together by non-covalent interactions such as hydrogen bonds and salt bridges hidden in the protein. The ligand has a phosphate group surrounded by polar amino acids, carbons are surrounded by non-polar amino acids to satisfy the needs of the ligand and active site. Interactions like hydrogen bonding and pi-stacking stabilize and bind the ligand in the active site.
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/>

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Carmen J Almendarez Rodriguez:

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<scene name='93/933999/Helix/2'>Text To Be Displayed</scene><scene name='93/933999/Amino_acid_300-304/1'>Text To Be Displayed</scene>{{Sandbox_Reserved_BHall_F22}}
==(hOAT')==
<StructureSection load='7T9Z' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page ''''''. 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:35460691</ref> to the rescue.

== Function of your protein == catalyzes the metabolic conversion of ornithine into an intermediate for proline or glutamate synthesis. Catalyzes the second step of the urea cycle, the condensation of carbamoyl phosphate with L-ornithine to form L-citrulline.

== Biological relevance and broader implications ==

== Important amino acids==
<scene name='93/933999/Amino_acid_300-304/1'>Amino Acids 300-304</scene> are an important part of protein binding <ref>PMID:35460691</ref>.
== Structural highlights ==
<scene name='93/933999/Helix/4'>An image of the helix in HOAT protein.</scene>
<scene name='93/933999/Ligands_of_interest/3'>The protein hOAT has three pyrodixal-5'phosphate ligands (PLP).<scene name='93/933999/Ligands_of_interest/1'></scene></scene>

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.
An image of the alpha carbon.

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

Sandbox Reserved 1755

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Carmen J Almendarez Rodriguez:

<scene name='93/933999/Helix/2'>Text To Be Displayed</scene><scene name='93/933999/Amino_acid_300-304/1'>Text To Be Displayed</scene>{{Sandbox_Reserved_BHall_F22}}
==(hOAT')==
<StructureSection load='7T9Z' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page ''''''. 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:35460691</ref> to the rescue.

== Function of your protein == catalyzes the metabolic conversion of ornithine into an intermediate for proline or glutamate synthesis. Catalyzes the second step of the urea cycle, the condensation of carbamoyl phosphate with L-ornithine to form L-citrulline.

== Biological relevance and broader implications ==

== Important amino acids==
<scene name='93/933999/Amino_acid_300-304/1'>Amino Acids 300-304</scene> are an important part of protein binding <ref>PMID:35460691</ref>.
== Structural highlights ==
<scene name='93/933999/Helix/4'>An image of the helix in HOAT protein.</scene>
The protein hOAT has three pyrodixal-5'phosphate ligands (PLP).<scene name='93/933999/Ligands_of_interest/1'></scene>

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.
An image of the alpha carbon.

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

Sandbox Reserved 1755

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Carmen J Almendarez Rodriguez:

<scene name='93/933999/Helix/2'>Text To Be Displayed</scene><scene name='93/933999/Amino_acid_300-304/1'>Text To Be Displayed</scene>{{Sandbox_Reserved_BHall_F22}}
==(hOAT')==
<StructureSection load='7T9Z' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page ''''''. 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:35460691</ref> to the rescue.

== Function of your protein == catalyzes the metabolic conversion of ornithine into an intermediate for proline or glutamate synthesis. Catalyzes the second step of the urea cycle, the condensation of carbamoyl phosphate with L-ornithine to form L-citrulline.

== Biological relevance and broader implications ==

== Important amino acids==
<scene name='93/933999/Amino_acid_300-304/1'>Amino Acids 300-304</scene> are an important part of protein binding <ref>PMID:35460691</ref>.
== Structural highlights ==
<scene name='93/933999/Helix/4'>An image of the helix in HOAT protein.</scene>

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.
An image of the alpha carbon.

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

Sandbox Reserved 1755

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Carmen J Almendarez Rodriguez:

<scene name='93/933999/Helix/2'>Text To Be Displayed</scene><scene name='93/933999/Amino_acid_300-304/1'>Text To Be Displayed</scene>{{Sandbox_Reserved_BHall_F22}}
==(hOAT')==
<StructureSection load='7T9Z' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page ''''''. 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:35460691</ref> to the rescue.

== Function of your protein == catalyzes the metabolic conversion of ornithine into an intermediate for proline or glutamate synthesis. Transferase. Homo sapiens. No mutations

== Biological relevance and broader implications ==

== Important amino acids==
<scene name='93/933999/Amino_acid_300-304/1'>Amino Acids 300-304</scene> are an important part of protein binding <ref>PMID:35460691</ref>.
== Structural highlights ==
<scene name='93/933999/Helix/4'>An image of the helix in HOAT protein.</scene>

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.
An image of the alpha carbon.

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

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Carmen J Almendarez Rodriguez:

<scene name='93/933999/Amino_acid_300-304/1'>Text To Be Displayed</scene>{{Sandbox_Reserved_BHall_F22}}
==(hOAT')==
<StructureSection load='7T9Z' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page ''''''. 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:35460691</ref> to the rescue.

== Function of your protein == catalyzes the metabolic conversion of ornithine into an intermediate for proline or glutamate synthesis. Transferase. Homo sapiens. No mutations

== Biological relevance and broader implications ==

== Important amino acids==
<scene name='93/933999/Amino_acid_300-304/1'>Amino Acids 300-304</scene> are an important part of protein binding <ref>PMID:35460691</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.

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

Sandbox Reserved 1755

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Carmen J Almendarez Rodriguez:

<scene name='93/933999/Amino_acid_300-304/1'>Text To Be Displayed</scene>{{Sandbox_Reserved_BHall_F22}}
==Your Heading Here (hOAT')==
<StructureSection load='7T9Z' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page ''''''. 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:35460691</ref> to the rescue.

== Function of your protein == catalyzes the metabolic conversion of ornithine into an intermediate for proline or glutamate synthesis. Transferase. Homo sapiens. No mutations

== Biological relevance and broader implications ==

== Important amino acids==
<scene name='93/933999/Amino_acid_300-304/1'>Amino Acids 300-304</scene> are an important part of protein binding <ref>PMID:35460691</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.

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

Sandbox Reserved 1755

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Carmen J Almendarez Rodriguez:

<scene name='93/933999/Amino_acid_300-304/1'>Text To Be Displayed</scene>{{Sandbox_Reserved_BHall_F22}}
==Your Heading Here (hOAT')==
<StructureSection load='7T9Z' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page ''''''. 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:35460691</ref> to the rescue.

== Function of your protein == catalyzes the metabolic conversion of ornithine into an intermediate for proline or glutamate synthesis

== Biological relevance and broader implications ==

== Important amino acids==
<scene name='93/933999/Amino_acid_300-304/1'>Amino Acids 300-304</scene> are an important part of protein binding <ref>PMID:35460691</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.

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

Sandbox Reserved 1755

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Carmen J Almendarez Rodriguez:

<scene name='93/933999/Amino_acid_300-304/1'>Text To Be Displayed</scene>{{Sandbox_Reserved_BHall_F22}}
==Your Heading Here (hOAT')==
<StructureSection load='7T9Z' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page ''''''. 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:35460691</ref> to the rescue.

== Function of your protein ==

== Biological relevance and broader implications ==

== Important amino acids==
<scene name='93/933999/Amino_acid_300-304/1'>Amino Acids 300-304</scene> are an important part of protein binding <ref>PMID:35460691</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.

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

Sandbox Reserved 1755

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Carmen J Almendarez Rodriguez:

<scene name='93/933999/Amino_acid_300-304/1'>Text To Be Displayed</scene>{{Sandbox_Reserved_BHall_F22}}
==Your Heading Here (hOAT')==
<StructureSection load='7T9Z' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page ''''''. 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 of your protein ==

== Biological relevance and broader implications ==

== Important amino acids==
<scene name='93/933999/Amino_acid_300-304/1'>Amino Acids 300-304</scene> are an important part of protein binding <ref>35460691</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.

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

Sandbox Reserved 1755

2022-11-20T04:23:46Z

Carmen J Almendarez Rodriguez:

<scene name='93/933999/Amino_acid_300-304/1'>Text To Be Displayed</scene>{{Sandbox_Reserved_BHall_F22}}
==Your Heading Here (hOAT')==
<StructureSection load='7T9Z' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page ''''''. 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 of your protein ==

== Biological relevance and broader implications ==

== Important amino acids==
<scene name='93/933999/Amino_acid_300-304/1'>Amino Acids 300-304</scene> are an important part of protein binding
== 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/>

Sandbox Reserved 1755

2022-11-20T03:14:42Z

Carmen J Almendarez Rodriguez: /* Your Heading Here (maybe something like 'Structure') */

{{Sandbox_Reserved_BHall_F22}}
==Your Heading Here (hOAT')==
<StructureSection load='7T9Z' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page ''''''. 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 of your protein ==

== Biological relevance and broader implications ==

== Important amino acids==

== 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/>

Sandbox Reserved 1755

2022-11-20T03:09:57Z

Carmen J Almendarez Rodriguez: /* Your Heading Here (maybe something like 'Structure') */