{{Sandbox_Reserved_BHall_F22}}
==Human ornithine aminotransferase (''h''OAT)==
<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.
[[Image:GABA.png|300 px|thumb|right|y-aminobutyric acid (GABA)]]
== Function of your protein ==
The specific function of <scene name='93/934005/Spin/2'>Human ornithine aminotransferase</scene> (''h''OAT) is that of an enzyme. It can be found in humans, as well as mice and pigs. It helps transfer L-ornithine’s δ-amino group to α-ketoglutarate (α-KG). <ref>https://doi.org/10.1016/j.jbc.2022.101969</ref> There is a lack of understanding in regards to ''h''OAT's catalytic mechanism, even though it is a key component of human metabolism. As noted in the article, ''h''OAT operates on a "Bi-Bi, Ping-Pong" kinetic mechanism resulting in the first part of the reaction undergoing a conversion of PLP -> PMP and L-Orn -> L-GSA. Then PMP's amino group is catalyzed by ''h''OAT creating an α-KG.
[[Image:Daba.png|300 px|thumb|right|L-2,4-diaminobutyric acid(DABA)]]

== Biological relevance and broader implications ==
''h''OAT is important because it is heavily involved in the urea cycle. In mammals, it dictates a large portion of the development of neonates. The research on this protein is relevant to science as a whole because it could directly impact cancer research and lead to the creation of cancer management in humans. There has been overexpression of ''h''OAT within Hepatocellular carcinoma (HCC) cells, therefore there is reason to believe that the overexpression of ''h''OAT is an indication of chronic liver diseases and cancer of the liver. The inhibitors include: y-aminobutyric acid (GABA), 5-aminovaleric acid (AVA), and L-2,4-diaminobutyric acid (DABA). The highest affinity of binding with ''h''OAT is GABA. It also has a higher percentage of return in the reverse reaction. The more that ''h''OAT is understood and researched, the more inactivators can be designed to combat the overexpression of ''h''OAT that is found in conjunction to HCC.

== Important amino acids==
The ligand of ''h''OAT is Pyridoxal-5'-Phosphate <scene name='93/934005/Plp/1'>(PLP)</scene>. The role of the catalytic amino acids in an enzyme is to bind to a substrate, changing the structure, causing bonds to break and new bonds to be formed. When there is a difficult reaction, the triad of amino acids works in tandem to facilitate the reaction. A <scene name='93/934005/Glu235/1'>Glu 235</scene>-<scene name='93/934005/Arg413/1'>Arg 413</scene> <scene name='93/934005/Arg_413_glu_235/1'>salt bridge</scene> was found on AVA, but not on GABA.

== Structural highlights ==

<scene name='93/934005/Main_secondary_features/1'>Main Secondary Features</scene>

<scene name='93/934005/Tert/1'>Tertiary/Quaternary Features</scene>
<scene name='93/934005/Space_fill_plp/1'>Space filling view of PLP</scene>
</StructureSection>

== References ==
<references/>
Butrin, A., Butrin, A., Wawrzak, Z., Moran, G. R., & Liu, D. (2022). Determination of the ph dependence, substrate specificity, and turnovers of alternative substrates for human ornithine aminotransferase. Journal of Biological Chemistry, 298(6), 101969. https://doi.org/10.1016/j.jbc.2022.101969

File:DABA.jpg

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Courtney Pierce:

File:GABA.png

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Courtney Pierce: drawing of GABA inhibitor

== Summary ==
drawing of GABA inhibitor
== Licensing ==
{{PD-self}}

Sandbox Reserved 1761

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Courtney Pierce:

{{Sandbox_Reserved_BHall_F22}}
==Human ornithine aminotransferase (''h''OAT)==
<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 specific function of <scene name='93/934005/Spin/2'>Human ornithine aminotransferase</scene> (''h''OAT) is that of an enzyme. It can be found in humans, as well as mice and pigs. It helps transfer L-ornithine’s δ-amino group to α-ketoglutarate (α-KG). <ref>https://doi.org/10.1016/j.jbc.2022.101969</ref> There is a lack of understanding in regards to ''h''OAT's catalytic mechanism, even though it is a key component of human metabolism. As noted in the article, ''h''OAT operates on a "Bi-Bi, Ping-Pong" kinetic mechanism resulting in the first part of the reaction undergoing a conversion of PLP -> PMP and L-Orn -> L-GSA. Then PMP's amino group is catalyzed by ''h''OAT creating an α-KG.

== Biological relevance and broader implications ==
''h''OAT is important because it is heavily involved in the urea cycle. In mammals, it dictates a large portion of the development of neonates. The research on this protein is relevant to science as a whole because it could directly impact cancer research and lead to the creation of cancer management in humans. There has been overexpression of ''h''OAT within Hepatocellular carcinoma (HCC) cells, therefore there is reason to believe that the overexpression of ''h''OAT is an indication of chronic liver diseases and cancer of the liver. The inhibitors include: y-aminobutyric acid (GABA), 5-aminovaleric acid (AVA), and L-2,4-diaminobutyric acid (DABA). The highest affinity of binding with ''h''OAT is GABA. It also has a higher percentage of return in the reverse reaction. The more that ''h''OAT is understood and researched, the more inactivators can be designed to combat the overexpression of ''h''OAT that is found in conjunction to HCC.

== Important amino acids==
The ligand of ''h''OAT is Pyridoxal-5'-Phosphate <scene name='93/934005/Plp/1'>(PLP)</scene>. The role of the catalytic amino acids in an enzyme is to bind to a substrate, changing the structure, causing bonds to break and new bonds to be formed. When there is a difficult reaction, the triad of amino acids works in tandem to facilitate the reaction. A <scene name='93/934005/Glu235/1'>Glu 235</scene>-<scene name='93/934005/Arg413/1'>Arg 413</scene> <scene name='93/934005/Arg_413_glu_235/1'>salt bridge</scene> was found on AVA, but not on GABA.

== Structural highlights ==

<scene name='93/934005/Main_secondary_features/1'>Main Secondary Features</scene>

<scene name='93/934005/Tert/1'>Tertiary/Quaternary Features</scene>
<scene name='93/934005/Space_fill_plp/1'>Space filling view of PLP</scene>
</StructureSection>

== References ==
<references/>
Butrin, A., Butrin, A., Wawrzak, Z., Moran, G. R., & Liu, D. (2022). Determination of the ph dependence, substrate specificity, and turnovers of alternative substrates for human ornithine aminotransferase. Journal of Biological Chemistry, 298(6), 101969. https://doi.org/10.1016/j.jbc.2022.101969

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Courtney Pierce:

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Courtney Pierce: adding cartoon

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Courtney Pierce: added biological relevance and functions

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