Literature summary for 1.6.3.5 extracted from

Beaupre, B.A.; Hoag, M.R.; Carmichael, B.R.; Moran, G.R.
Kinetics and equilibria of the reductive and oxidative half-reactions of human renalase with alpha-NADPH (2013), Biochemistry, 52, 8929-8937.

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Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q5VYX0	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
alpha-NAD(P)H + H+ + O2	-	Homo sapiens	beta-NAD(P)+ + H2O2	renalase is selective for the alpha-anomer, which binds with a dissociation constant of about 20 microM. This association precedes monophasic two-electron reduction of the FAD cofactor with a rate constant of 40.2 per s. The reduced enzyme then delivers both electrons to dioxygen in a second-order reaction with a rate constant of about 2900 per M and s. Renalase has modest affinity for its beta-NADP+ product, and the FAD cofactor has a reduction potential of -155 mV that is unaltered by saturating beta-NADP+. Data suggest that the products are formed and released in a kinetically ordered sequence, first beta-NADP+ then H2O2	?

Cofactor

Cofactor	Comment	Organism	Structure
FAD	the FAD cofactor has a reduction potential of ?155 mV that is unaltered by saturating beta-NADP+	Homo sapiens

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Release 2023.1 (January 2023)