Literature summary for 2.6.1.13 extracted from

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

Search for more literature for 2.6.1.13

Inhibitors

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

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	-	-	-

Substrates and Products (Substrate)

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

Temperature Optimum [°C]

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

Cofactor

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

Ki Value [mM]

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

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Release 2023.1 (January 2023)