Sandbox Reserved 1761

This Sandbox is Reserved from November 4, 2022 through January 1, 2023 for use in the course CHEM 351 Biochemistry taught by Bonnie Hall at the Grand View University, Des Moines, USA. This reservation includes Sandbox Reserved 1755 through Sandbox Reserved 1764.

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Human ornithine aminotransferase (hOAT)

spinqualitylabelsall models Caption for this structure Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D 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 or to the article describing Jmol to the rescue. Function of your protein The specific function of Human ornithine aminotransferase (hOAT) 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). Rotating cartoon Biological relevance and broader implications hOAT 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 hOAT within Hepatocellular carcinoma (HCC) cells, therefore there is reason to believe that the overexpression of hOAT is an indication of chronic liver diseases and cancer of the liver. Important amino acids The ligand of hOAT is Pyridoxal-5'-Phosphate (PLP). Amino acids include y-aminobutyric acid (GABA), 5-aminovaleric acid (AVA), and L-2,4-diaminobutyric acid (DABA). The highest affinity of binding with hOAT is GABA. It also has a higher percentage of return in the reverse reaction. 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. Structural highlights Main Secondary Features Tertiary/Quaternary Features

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