EC Number   |
Application |
Reference |
|---|
    2.6.1.13 | agriculture |
expression of enzyme in Oryza sativa, transgenic plants are significantly taller than control, and more resistant to high salinity and drought |
663174 |
| 2.6.1.13 | analysis |
development of two new continuous, coupled assays for ornithine-delta-aminotransferase (OAT) that are more sensitive than previous methods, measure activity in real time, and can be carried out in multi-well plates for convenience and high throughput. The first assay is based on the reduction of DELTA1-pyrroline-5-carboxylate (P5C), generated from ornithine by OAT, using human pyrroline 5-carboxylate reductase 1, which results in the concomitant oxidation of NADH to NAD+. This procedure is three times more sensitive than previous methods, and is suitable for the study of small molecules as inhibitors or inactivators of OAT or as a method to determine OAT activity in unknown samples. The second method involves the detection of L-glutamate, produced during the regeneration of the cofactor PLP of OAT by an unamplified modification of the commercially available Amplex® Red L-glutamate detection kit (Life Technologies). This assay is recommended for the determination of the substrate activity of small molecules against OAT |
737430 |
| 2.6.1.13 | biotechnology |
genetic engineering of plants for increased production of the osmoprotectant proline, transgenic plants overexpressing OAT display enhanced tolerance to salt and drought due to increased proline content |
706356 |
| 2.6.1.13 | diagnostics |
OAT may be a potential biomarker for the diagnosis and therapeutic outcome monitoring of non-small cell lung cancer (NSCLC). Relationship between OAT mRNA expression and clinicopathological features in patients with NSCLC, overview |
759545 |
| 2.6.1.13 | diagnostics |
the standardization of the enzyme kinetics can be extended to detect enzyme activity in patients of gyrate atrophy of choroid and retina with hyperornithinemia by studying the OAT activity |
703993 |
| 2.6.1.13 | drug development |
because TgOAT possesses parasite-specific structural features as well as differing substrate specificity from its human homologue, it is an attractive target for anti-toxoplasmosis inhibitor design that can be exploited for chemotherapeutic intervention |
-, 758756 |
| 2.6.1.13 | drug development |
human OAT as a potential target for development of new therapeutic drugs, OAT holds a significant scientific interest because of its association with gyrate atrophy, a recessive hereditary genetic dissorder leading to progressive loss of vision and eventually blindness in humans |
706356 |
| 2.6.1.13 | drug development |
human OAT is recognized as a potential target for chemotherapeutic drug development, in a study performed to evaluate the effect of selective blocking of mitosis in human cancer cells, OAT is identified as a protein, which binds the antimitotic drug diazonamide A and it has a role in regulating mitotic cell division |
706356 |
| 2.6.1.13 | medicine |
before puberty, ornithine aminotransferase expression is similar between female and male kidneys whereas from puberty until adulthood ornithine aminotransferase expression increases in the female kidney, becoming 2.5fold higher than in the male kidney. This sex-differential expression of ornithine aminotransferase is associated with a sex-specific distribution of enzyme along the corticopapillary axis and within the nephron. Ornithine aminotransferase is three- to fourfold more expressed in the female than the male cortex. In males, enzyme is highly expressed in the medulla, mainly in the thick ascending limbs. Renal enzyme distribution in orchidectomized mice resembles that in the females. Ovariectomy does not influence enzyme expression. Ornithine aminotransferase is naturally downregulated in the presence of testosterone |
671263 |
| 2.6.1.13 | medicine |
in rats, a liver portacaval shunt causes a marked decrease in glutamine synthetase activity and an increase in ornithine aminotransferase activity. The glutamine synthetase and ornithine aminotransferase proteins maintain their location in the perivenous cells, indicating that there is no generalized loss of perivenous hepatocytes, but rather, there is a significant alteration in the expression of these proteins and hence metabolism in this cell population |
737967 |
