EC Number   |
General Information |
Reference |
|---|
    2.6.1.62 | evolution |
the enzyme belongs to class III of the superfamily of aminotransferases (transaminase, TA) |
-, 758685 |
| 2.6.1.62 | malfunction |
deletion of the gabT gene encoding GABA-T cannot prevent GABA from decomposing at neutral pH. An additional transaminase gene, NCgl2515, is deleted in a gabT-deleted GAD strain, but the GABA concentration in this gabT-deleted GAD strain NCgl2515 remains unaltered when pH is maintained at pH 7.5-8.0, demonstrating that GABA decomposition is reduced |
-, 760076 |
| 2.6.1.62 | metabolism |
enzyme 7,8-diaminopelargonic acid aminotransferase (BioA) in Mycobacterium tuberculosis is primarily involved in the lipid biosynthesis pathway |
-, 756558 |
| 2.6.1.62 | metabolism |
unlike GabT (EC 2.6.1.19), which exhibits high GABA-T activity and utilizes only 2-oxoglutarate as amino acceptor, the purified NCgl2515 protein exhibits very low GABA-T activity only when coupled with succinate-semialdehyde dehydrogenase (SSADH), GabD, but can utilize both 2-oxoglutarate and pyruvate as amino acceptor |
-, 760076 |
| 2.6.1.62 | more |
the conversion of amines is a promiscuous activity of many transaminases of class III and is independent from their natural function. Molecular docking calculations of S-adenosyl-L-methionine, (S)-(-)-1-phenylethylamine, and its quinonoid intermediates in the active site of the enzyme |
-, 758685 |
