CATH Classification

Domain Context

CATH Clusters

Superfamily Cytochrome P450
Functional Family Bifunctional cytochrome P450/NADPH--P450 reductase

Enzyme Information

1.6.2.4
NADPH--hemoprotein reductase.
based on mapping to UniProt P14779
NADPH + n oxidized hemoprotein = NADP(+) + n reduced hemoprotein.
-!- This enzyme catalyzes the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P450 monooxygenases (e.g. EC 1.14.14.1) by stabilizing the one-electron reduced form of the flavin cofactors FAD and FMN. -!- It also reduces cytochrome b5 and cytochrome c. -!- The number n in the equation is 1 if the hemoprotein undergoes a 2-electron reduction, and is 2 if it undergoes a 1-electron reduction.
1.14.14.1
Unspecific monooxygenase.
based on mapping to UniProt P14779
RH + [reduced NADPH--hemoprotein reductase] + O(2) = ROH + [oxidized NADPH--hemoprotein reductase] + H(2)O.
-!- Acts on a wide range of substrates including many xenobiotics, steroids, fatty acids, vitamins and prostaglandins; reactions catalyzed include hydroxylation, epoxidation, N-oxidation, sulfooxidation, N-, S- and O-dealkylations, desulfation, deamination, and reduction of azo, nitro and N-oxide groups. -!- Together with EC 1.6.2.4, it forms a system in which two reducing equivalents are supplied by NADPH. -!- Some of the reactions attributed to EC 1.14.15.3 belong here. -!- Formerly EC 1.14.1.1, EC 1.14.14.2, EC 1.14.99.8 and EC 1.99.1.1.

UniProtKB Entries (1)

P14779
CPXB_BACMB
Bacillus megaterium NBRC 15308 = ATCC 14581
Bifunctional cytochrome P450/NADPH--P450 reductase

PDB Structure

PDB 1JME
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Structural and spectroscopic analysis of the F393H mutant of flavocytochrome P450 BM3.
Ost, T.W., Munro, A.W., Mowat, C.G., Taylor, P.R., Pesseguiero, A., Fulco, A.J., Cho, A.K., Cheesman, M.A., Walkinshaw, M.D., Chapman, S.K.
Biochemistry