Cytochrome P450 BM3
| Bifunctional cytochrome P450/NADPH--P450 reductase | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Organism | |||||||
| Symbol | P450BM3 | ||||||
| Alt. symbols | CYP102A1 | ||||||
| PDB | 2IJ2 | ||||||
| RefSeq (mRNA) | NZ_JJMH01000056.1 | ||||||
| RefSeq (Prot) | WP_034650526.1 | ||||||
| UniProt | P14779 | ||||||
| Other data | |||||||
| EC number | 1.6.2.4 | ||||||
| |||||||
Cytochrome P450 BM3 is a Prokaryote Cytochrome P450 enzyme originally from Bacillus megaterium catalyzes the hydroxylation of several long-chain fatty acids at the ω–1 through ω–3 positions. This bacterial enzyme belongs to CYP family CYP102, with the CYP Symbol CYP102A1.This CYP family constitutes a natural fusion between the CYP domain and an NADPH-dependent cytochrome P450 reductase.[1][2]
References
[edit]- ^ Narhi LO, Fulco AJ (June 1986). "Characterization of a catalytically self-sufficient 119,000-dalton cytochrome P-450 monooxygenase induced by barbiturates in Bacillus megaterium". The Journal of Biological Chemistry. 261 (16): 7160–9. doi:10.1016/S0021-9258(17)38369-2. PMID 3086309.
- ^ Girvan HM, Waltham TN, Neeli R, Collins HF, McLean KJ, Scrutton NS, Leys D, Munro AW (December 2006). "Flavocytochrome P450 BM3 and the origin of CYP102 fusion species". Biochemical Society Transactions. 34 (Pt 6): 1173–7. doi:10.1042/BST0341173. PMID 17073779.
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