Literature summary for 1.14.13.242 extracted from

Kishore, G.M.; Snell, E.E.
Kinetic investigations on a flavoprotein oxygenase, 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase (1981), J. Biol. Chem., 256, 4228-4233.

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Inhibitors

Inhibitors	Comment	Organism	Structure
NAD+	binds competitively with O2, but not with NADH	Pseudomonas sp.

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas sp.	-	MA-1	-

Reaction

Reaction	Comment	Organism	Reaction ID
3-hydroxy-2-methylpyridine-5-carboxylate + NAD(P)H + H+ + O2 = 2-(acetamidomethylidene)succinate + NAD(P)+	ordered mechanism in which 3-hydroxy-2-methylpyridine-5-carboxylate binds first, followed by NADH. The first product NAD+ is then released, followed by oxygen binding and finally release of the oxygenated and reduced cleavage product 2-(acetamidomethylene)succinate	Pseudomonas sp.	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2	-	Pseudomonas sp.	2-(acetamidomethylene)succinate + NAD(P)+	-	?

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
additional information	-	additional information	-	Pseudomonas sp.

Cofactor

Cofactor	Comment	Organism	Structure
NADH	-	Pseudomonas sp.

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Release 2023.1 (January 2023)