Literature summary for 1.14.13.59 extracted from

Macheroux, P.; Plattner, H.J.; Romaguera, A.; Diekmann, H.
FAD and substrate analogs as probes for lysine N6-hydroxylase from Escherichia coli EC 222 (1993), Eur. J. Biochem., 213, 995-1002.

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Inhibitors

Inhibitors	Comment	Organism	Structure
FAD analogs	complete loss of activity after prolonged incubation with 8-chloro-FAD, 8-fluoro-FAD, 8-mercapto-FAD or 8-methoxy-FAD	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-Lys + NADPH + O2	-	Escherichia coli	N6-Hydroxy-L-Lys + NADP+ + H2O	-	?
additional information	in absence of substrate, the enzyme has an NADPH oxidase activity which results in generation of H2O2	Escherichia coli	?	-	?

Cofactor

Cofactor	Comment	Organism	Structure
FAD	requires FAD	Escherichia coli
FAD	binding is very weak	Escherichia coli
FAD	Km: 0.0007 mM	Escherichia coli
NADPH	required	Escherichia coli

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Release 2023.1 (January 2023)