EC Number   |
Natural Substrates |
|---|
   1.11.2.4 | 3,5,3',5'-tetramethylbenzidine + H2O2 |
a myristic acid-dependent reaction, when deuterated myristic acid is used as a substrate to decrease hydroxylation activity, the rate of 3,5,3',5'-tetramethylbenzidine oxidation increases |
| 1.11.2.4 | fatty acid + H2O2 |
- |
| 1.11.2.4 | more |
a reductase and NAD(P)H are not required for activity |
| 1.11.2.4 | more |
CYP152A2 has a clear preference for hydroxylation at alpha-position |
| 1.11.2.4 | more |
P450 BM-3 peroxygenase 21B3 is a laboratory-evolved variant of the P450 BM-3 heme domain which functions as an H2O2-driven hydroxylase (peroxygenase) and does not require NADPH, O2 , or the reductase |
| 1.11.2.4 | more |
P450BSbeta produces alpha- and beta-hydroxylated products at 33 and 67%, respectively |
| 1.11.2.4 | more |
P450BSbeta produces both the beta-OH (60%) and the alpha-OH (40%) fatty acids. Ferredoxin, ferredoxin reductase, and P450 reductase systems do not appear to function in P450BSbeta reactions. P450BSbeta does not require any electrons and protons for catalytic activity, because it utilizes H2O2 as an oxidant instead of O2/2e-/2H+. This enzyme requires neither a reductase nor a proton delivery system |
| 1.11.2.4 | more |
P450SPalpha produces the alpha-hydroxylated products at 100% |
| 1.11.2.4 | more |
the enzyme catalyzes the subterminal (omega-1 to omega-3) hydroxylation of fatty acids. The enzyme can complete its function without the aid of other proteinaceous components such as NADPH-cytochrome P450 oxidoreductase |
| 1.11.2.4 | more |
the enzyme never requires a supply of electrons or protons |
