Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | Q5VYX0 | - |
- |
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 | Comment | Organism | Structure |
---|---|---|---|
FAD | the FAD cofactor has a reduction potential of ?155 mV that is unaltered by saturating beta-NADP+ | Homo sapiens |