Sandbox Reserved 1761: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 7: | Line 7: | ||
== Function of your protein == | == 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. | 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.jpg| | [[Image:Daba.jpg|200 px|thumb|right|DABA]] | ||
== Biological relevance and broader implications == | == Biological relevance and broader implications == | ||
