2.6.1.13: ornithine aminotransferase
This is an abbreviated version!
For detailed information about ornithine aminotransferase, go to the full flat file.
Word Map on EC 2.6.1.13
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2.6.1.13
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atrophy
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gyrate
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arginase
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retina
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choroid
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pyridoxal
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polyamines
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chorioretinal
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hyperornithinemia
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citrulline
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putrescine
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transamination
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aminotransferases
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delta1-pyrroline-5-carboxylate
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1-pyrroline-5-carboxylate
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argininosuccinate
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gabaculine
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hyperammonemias
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carbamoylphosphate
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biotechnology
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medicine
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plp-dependent
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analysis
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drug development
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diagnostics
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agriculture
- 2.6.1.13
- atrophy
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gyrate
- arginase
- retina
- choroid
- pyridoxal
- polyamines
-
chorioretinal
-
hyperornithinemia
- citrulline
- putrescine
-
transamination
- aminotransferases
- delta1-pyrroline-5-carboxylate
- 1-pyrroline-5-carboxylate
- argininosuccinate
- gabaculine
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hyperammonemias
- carbamoylphosphate
- biotechnology
- medicine
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plp-dependent
- analysis
- drug development
- diagnostics
- agriculture
Reaction
Synonyms
aminotransferase, ornithine-keto acid, delta OAT, delta-OAT, delta-ornithine aminotransferase, deltaOAT, EC 2.6.1.68, hOAT, L-ornithine 5-aminotransferase, L-ornithine aminotransferase, L-ornithine:2-oxoacid aminotransferase, L-ornithine:alpha-ketoglutarate delta-aminotransferase, OAT, Orn-AT, ornithine 5-aminotransferase, ornithine amino transferase, ornithine aminotransferase, ornithine delta aminotransferase, ornithine delta-amino transferase, ornithine delta-aminotransferase, ornithine delta-transaminase, ornithine transaminase, ornithine-2-oxoacid aminotransferase, ornithine-alpha-ketoglutarate aminotransferase, ornithine-delta-aminotransferase, ornithine-keto acid aminotransferase, ornithine-keto acid transaminase, ornithine-ketoglutarate aminotransferase, ornithine-oxo acid aminotransferase, ornithine-oxo-acid transaminase, ornithine: 2-oxo-glutarate aminotransferase, ornithine:alpha-oxoglutarate transaminase, PsOAT, RocD, TaOAT, TaOAT-5AL, TaOAT-5B, TaOAT-5BL, TaOAT-5DL, TaOAT-AL-2, TgOAT
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Application on EC 2.6.1.13 - ornithine aminotransferase
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APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
agriculture
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expression of enzyme in Oryza sativa, transgenic plants are significantly taller than control, and more resistant to high salinity and drought
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
biotechnology
diagnostics
drug development
medicine
biotechnology
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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
biotechnology
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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
biotechnology
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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
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
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
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
diagnostics
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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
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
drug development
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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
drug development
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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
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
drug development
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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
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drug development
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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
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medicine
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patient with gyrate atrophy of the choroid and retina, mutation G237D, responds to vitamin B6 medication
medicine
pharmacological doses of testosterone down-regulate level of enzyme protein. Variations of levels of enzyme are strongly correlated with testosteronemia. Orchidectomy increases renal level of enzyme protein. Effects are reversed by injecting physiological doses of testosterone into castrated male animals
medicine
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role in mitotic cell division and target for chemotherapeutic drug development
medicine
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role in mitotic cell division and target for chemotherapeutic drug development
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
medicine
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transgenic mice that specifically overexpress human ornithine aminotransferase in the liver, kidneys and intestine exhibit higher enzyme activity in the liver than wild-type, but there are no differences in kinetic parameters between wild-type and transgenic animal. Ornithine aminotransferase overexpression decreases plasma and liver ornithine concentrations but does not affect glutamine or arginine homeostasis. There is an inverse relationship between ornithine levels and enzyme activity
medicine
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transgenic mice that specifically overexpress human ornithine aminotransferase in the liver, kidneys and intestine exhibit higher enzyme activity in the liver than wild-type, but there are no differences in kinetic parameters between wild-type and transgenic animal. Ornithine aminotransferase overexpression decreases plasma and liver ornithine concentrations but does not affect glutamine or arginine homeostasis. There is an inverse relationship between ornithine levels and enzyme activity
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
medicine
inhibition of OAT may represent a therapeutic strategy in treatment of non-small cell lung cancer (NSCLC)
