EC Number |
General Information |
Reference |
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2.6.1.13 | malfunction |
a deficit in ornithine aminotransferase (OAT) is associated with gyrate atrophy, a rare autosomal recessive disorder causing progressive blindness and chorioretinal degeneration |
760090 |
2.6.1.13 | metabolism |
catalyzes step 5 in the ornithine fermentation pathway |
704292 |
2.6.1.13 | malfunction |
deltaOAT and proline dehydrogenases (ProDH1 and ProDH2) are involved in the defence against non-host pathogens. Mutants for these genes compromise non-host resistance and show a decrease in non-host pathogen-induced reactive oxygen species |
723382 |
2.6.1.13 | malfunction |
deltaOAT and proline dehydrogenases (ProDH1 and ProDH2) are involved in the defence against non-host pathogens. Silencing of these genes in Nicotina benthamiana delays occurrence of hypersensitive response and favours non-host pathogen growth |
723382 |
2.6.1.13 | physiological function |
deltaOAT is involved in effector-triggered immunity (ETI) and plays a critical role in inducing early oxidative burst and other defence pathways in plants, conceivably by accumulating P5C in mitochondria |
723382 |
2.6.1.13 | physiological function |
enzyme is implicated in salt tolerance in higher plants, enzyme is implicated in proline biosynthesis and accumulation via pyrroline-5-carboxylate |
706356 |
2.6.1.13 | physiological function |
enzyme is implicated in salt tolerance in higher plants, enzyme is implicated in proline biosynthesis and accumulation via pyrroline-5-carboxylate, OAT is essential for nitrogen recycling from arginine but not for the stress-induced proline accumulation, OAT probably links the degradation pathways for arginine and proline |
706356 |
2.6.1.13 | physiological function |
human ornithine aminotransferase (hOAT), a pyridoxal 5'-phosphate-dependent enzyme, plays a critical role in the progression of hepatocellular carcinoma (HCC) and in the metabolic reprograming of HCC via proline and glutamine metabolic pathways |
759413 |
2.6.1.13 | physiological function |
in the presence of arginine, Mycobacterium tuberculosis upregulates a gene cluster which includes ornithine aminotransferase (rocD) and Rv2323c, a gene of up to now unknown function. In Mycobacterium tuberculosis, arginine is not only used as nitrogen source but also as carbon source for the formation of amino acids, in particular of proline. RocD is naturally deleted in Mycobacterium tuberculosis, but not in non-tuberculous mycobacteria. Mycobacterium tuberculosis lacking gene Rv2323c shows a growth defect on arginine, does not produce proline from arginine, and incorporates less nitrogen derived from arginine in its core nitrogen metabolism |
-, 739425 |
2.6.1.13 | physiological function |
increased OAT activity and ornithine concentration can impact the supply of substrates for proline synthesis |
723051 |