Literature summary for 1.14.13.1 extracted from

Suzuki, K.; Mizuguchi, M.; Gomi, T.; Itagaki, E.
Identification of a lysine residue in the NADH-binding site of salicylate hydroxylase from Pseudomonas putida S-1 (1995), J. Biochem., 117, 579-585.

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Inhibitors

Inhibitors	Comment	Organism	Structure
Trinitrobenzenesulfonic acid	irreversible inactivation, modification of a lysine residue results in loss of NADH-dehydrogenase activity suggesting its role in the NADH-binding site of the enzyme	Pseudomonas putida

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.0016	-	salicylate	native enzyme	Pseudomonas putida
0.0018	-	salicylate	modified enzyme	Pseudomonas putida
0.0037	-	NADH	native enzyme	Pseudomonas putida
0.049	-	NADH	modified enzyme	Pseudomonas putida

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas putida	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
salicylate + NADH + H+ + O2	-	Pseudomonas putida	catechol + NAD+ + H2O + CO2	-	?

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Release 2023.1 (January 2023)