EC Number   |
General Information |
Reference |
|---|
    2.6.1.13 | malfunction |
mutation of Val79 to Tyr results in a change of substrate preference between GABA, N-acetylornithine and L-ornithine, suggesting a key role of Val79 in defining substrate specificity |
-, 758756 |
| 2.6.1.13 | metabolism |
OAT plays a different role in arginine, ornithine and proline metabolism depending on the tissue and their physiological needs |
703993 |
| 2.6.1.13 | physiological function |
ornithine aminotransferase (OAT) promotes the proliferation, invasion, and migration, inhibits the apoptosis, and alters cell cycle of non-small cell lung cancer cells (NSCLC cells). Also the involvement of OAT-miR-21-glycogen synthase kinase-3beta signaling in the functional role of OAT in NSCLC is revealed. Glycogen synthase kinase-3beta (GSK-3beta) is a direct target of miR-21 in NSCLC |
759545 |
| 2.6.1.13 | evolution |
ornithine aminotransferase is a highly conserved enzyme present in all prokaryotes and eukaryotes, from unicellular bacteria to multicellular animals and plants. In Triticum aestivum, three homeologous OAT genes in wheat genome are found on chromosome group 5, named as TaOAT-5AL, TaOAT-5BL, and TaOAT-5DL. The phylogenetic tree indicates that OATs share highly conserved domains between monocotyledons and eudicotyledons |
758976 |
| 2.6.1.13 | evolution |
ornithine aminotransferase is a highly conserved enzyme present in all prokaryotes and eukaryotes, from unicellular bacteria to multicellular animals and plants. In Triticum aestivum, three homeologous OAT genes in wheat genome are found on chromosome group 5, named as TaOAT-5AL, TaOAT-5BL, and TaOAT-5DL. Two transcript variants of TaOAT-5AL are revealed, named TaOAT-5AL-1 and TaOAT-5AL-2 and characterized by 1497 bp and 1287 bp in cDNA length, respectively. Compared to TaOAT-5AL-2, TaOAT-5AL-1 contains an additional 120-bp insertion encompassing an in-frame stop codon, which resulted in a premature protein. The additional insertion is genotypically confirmed by sequencing results from six cultivars. The phylogenetic tree indicates that OATs share highly conserved domains between monocotyledons and eudicotyledons |
758976 |
| 2.6.1.13 | physiological function |
ornithine delta-aminotransferase (OAT) is a pyridoxal 5'-phosphate (PLP)-dependent enzyme that catalyzes the delta-transamination of L-ornithine and 2-oxoglutarate to glutamic-gamma-semialdehyde (GSA) and L-glutamate in the mitochondrial matrix. GSA then spontaneously cyclizes forming pirroline-5-carboxylate (P5C), a proline precursor |
760090 |
| 2.6.1.13 | physiological function |
ornithine-delta-aminotransferase OAT is essential for Xenopus embryonic development, and overexpression of OAT produces a ventralized phenotype characterized by a small head, lack of axial structure, and defective expression of neural developmental markers. Substitution of both Arg 180 and Leu 402 abrogates both OAT enzymatic activity and ability to modulate the developmental phenotype. Neurogenesis is inhibited by OAT during Xenopus embryonic development |
738432 |
| 2.6.1.13 | malfunction |
overexpression of OAT promotes the growth and metastasis of A-549 lung cancer cells, and overexpression of OAT also promotes the epithelial-mesenchymal transition (EMT) of OAT-overexpressing A549 cells. Knockdown of OAT inhibits the proliferation and metastasis of H-1299 cells |
759545 |
| 2.6.1.13 | malfunction |
selective inhibition of hOAT has been shown to effectively suppress hepatocellular carcinoma (HCC) tumor growth in vivo |
759413 |
| 2.6.1.13 | physiological function |
the Corynebacterium glutamicum ornithine acetyltransferase (OATase) ArgJ strongly influences the production of L-ornithine by OAT in Corynebacterium glutamicum |
-, 756237 |
