Literature summary for 1.11.1.1 extracted from

Crane, E.J.; Parsonage, D.; Poole, L.B.; Claiborne, A.
Analysis of the kinetic mechanism of enterococcal NADH peroxidase reveals catalytic roles for NADH complexes with both oxidized and two-electron-reduced enzyme forms (1995), Biochemistry, 34, 14114-14124.

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Enterococcus faecalis

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	Km values over a pH range from pH 5.5 to pH 8.5	Enterococcus faecalis

Organism

Organism	UniProt	Comment	Textmining
Enterococcus faecalis	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Enterococcus faecalis

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
NADH + H2O2	detailed reaction mechanism	Enterococcus faecalis	NAD+ + H2O	-	?

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
additional information	-	additional information	pH dependence of kcat from pH 5 to pH 9	Enterococcus faecalis

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Release 2023.1 (January 2023)