Literature summary extracted from

Hano, N.; Nakashima, Y.; Shinzawa-Itoh, K.; Terada, H.; Yoshikawa, S.
Effect of pH on the steady state kinetics of bovine heart NADH:coenzyme Q oxidoreductase (2003), J. Bioenerg. Biomembr., 35, 419-425.

KM Value [mM]

EC Number	KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
7.1.1.2	additional information	-	additional information	Km-values for decylubiquinone are measured at pH-values 6.5 and 9.0 at different concentrations of the cosubstrate NADH. Km-values for NADH are measured at pH values 6.5, 7.0, 7.5, 8.0, 8.5 and 9.0 and at different concentrations of the cosubstrate decylubiquinone	Bos taurus

Organism

EC Number	Organism	UniProt	Comment	Textmining
7.1.1.2	Bos taurus	-	-	-

Source Tissue

EC Number	Source Tissue	Comment	Organism	Textmining
7.1.1.2	heart	-	Bos taurus	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
7.1.1.2	NADH + decylubiquinone	ordered sequential mechanism in which the order of substrate bindings and product release is: NADH, decylubiquinone, decylubiquinol, NAD+	Bos taurus	NAD+ + decylubiquinol	-	?

Synonyms

EC Number	Synonyms	Comment	Organism
7.1.1.2	NADH:coenzyme Q oxidoreductase	-	Bos taurus

pH Range

EC Number	pH Minimum	pH Maximum	Comment	Organism
7.1.1.2	additional information	-	only NADH binding to the enzyme in pH-dependent. NADH binding to the free enzyme is accelerated by protonation of an amino acid (possibly His)	Bos taurus

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
7.1.1.2	NADH	-	Bos taurus

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Release 2023.1 (January 2023)