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 4KPA
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structural Evidence: A Single Charged Residue Affects Substrate Binding in Cytochrome P450 BM-3.
Catalano, J., Sadre-Bazzaz, K., Amodeo, G.A., Tong, L., McDermott, A.
Biochemistry
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