EC Number   |
Substrates |
Organism  |
Products |
Reversibility |
|---|
   1.6.3.5 | 1,2-dihydro-beta-NADH + H+ + O2 |
- |
Homo sapiens |
beta-NAD+ + H2O2 |
- |
? |
| 1.6.3.5 | 1,2-dihydro-beta-NADPH + H+ + O2 |
- |
Homo sapiens |
beta-NADP+ + H2O2 |
- |
? |
| 1.6.3.5 | 1,6-dihydro-beta-NADH + H+ + O2 |
- |
Homo sapiens |
beta-NAD+ + H2O2 |
- |
? |
| 1.6.3.5 | 1,6-dihydro-beta-NADPH + H+ + O2 |
- |
Homo sapiens |
beta-NADP+ + H2O2 |
- |
? |
| 1.6.3.5 | 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 |
? |
| 1.6.3.5 | alpha-NAD(P)H + H+ + O2 |
renalase is a protein hormone secreted into the blood by the kidney that is reported to lower blood pressure and slow heart rate |
Homo sapiens |
beta-NAD(P)+ + H2O2 |
- |
? |
| 1.6.3.5 | alpha-NAD(P)H + H+ + O2 |
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 |
Homo sapiens |
beta-NAD(P)+ + H2O2 |
- |
? |
| 1.6.3.5 | alpha-NADH + H+ + O2 |
- |
Homo sapiens |
beta-NAD+ + H2O2 |
- |
? |
| 1.6.3.5 | alpha-NADPH + H+ + O2 |
- |
Homo sapiens |
beta-NADP+ + H2O2 |
- |
? |
| 1.6.3.5 | catecholamine + O2 |
- |
Homo sapiens |
oxidized catecholamine + H2O2 |
- |
? |
