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Literature summary extracted from

  • Kito, K.; Sanada, Y.; Katunuma, N.
    Mode of inhibition of ornithine aminotransferase by L-canaline (1978), J. Biochem., 83, 201-206.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.6.1.13 5-Aminopentanoate 5-aminovaleric acid Rattus norvegicus
2.6.1.13 hydroxylamine reversible, noncompetitive Rattus norvegicus
2.6.1.13 L-canaline i.e. 2-amino-4-(aminooxy)-n-butanoic acid, irreversible, forms oxime-type compound with pyridoxal 5'-phosphate Rattus norvegicus
2.6.1.13 N2-Acetyl-L-ornithine competitive with L-ornithine Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
2.6.1.13 Rattus norvegicus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.6.1.13 L-ornithine + 2-oxoglutarate
-
Rattus norvegicus DELTA1-pyrroline-5-carboxylate + L-glutamate
-
?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.6.1.13 37
-
assay at Rattus norvegicus

Cofactor

EC Number Cofactor Comment Organism Structure
2.6.1.13 pyridoxal 5'-phosphate a pyridoxal phosphate protein Rattus norvegicus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.6.1.13 0.00043
-
hydroxylamine pH 8, 37°C Rattus norvegicus
2.6.1.13 0.0017
-
5-Aminopentanoate pH 8, 37°C Rattus norvegicus
2.6.1.13 0.0088
-
N2-L-acetyl ornithine pH 8, 37°C Rattus norvegicus