1.6.3.5	FAD	-	741574, 741775, 741785, 741788, 741869, 741913, 741920, 742004, 742685, 743215	
1.6.3.5	FAD	flavoprotein. The substrate alpha-dihydropyridyl ring is oxidized by transferring two electrons to the flavin cofactor and the configuration of the ribose C1 is converted from alpha to beta. The reduced FAD cofactor then reoxidizes by reacting with dioxygen to yield hydrogen peroxide	725209	
1.6.3.5	FAD	only extracellular (circulating) renalase acts in a FAD-independent manner	743189	
1.6.3.5	FAD	the FAD cofactor has a reduction potential of ?155 mV that is unaltered by saturating beta-NADP+	727037	
1.6.3.5	FAD	the FAD prosthetic group becomes slowly reduced when the enzyme is incubated with NADPH under anaerobiosis	728146	
1.6.3.5	additional information	a recognizable NADP-binding site is absent in the protein structure, enzyme shows poor affinity for, and poor reactivity towards, NADH and NADPH with Kd values of ca 2 mM	728146	
1.6.3.5	NADH	-	741574, 741775, 741785, 741788, 741869, 741902, 741913, 741920, 742004, 743215	
1.6.3.5	NADPH	-	741775, 741785, 741788, 741869, 741902, 741913, 741920, 742004, 743215