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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). ^[3]

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.^[4]

Important amino acids

The ligand of hOAT is Pyridoxal-5'-Phosphate . 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.^[5]

Structural highlights

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