Biology:Cytochrome P450 BM3
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Short description: Enzyme
| Bifunctional cytochrome P450/NADPH--P450 reductase | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Organism | |||||||
| Symbol | P450BM3 | ||||||
| Alt. symbols | CYP102A1 | ||||||
| PDB | 2IJ2 (ECOD) | ||||||
| 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
- ↑ "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. June 1986. doi:10.1016/S0021-9258(17)38369-2. PMID 3086309. http://www.jbc.org/cgi/pmidlookup?view=long&pmid=3086309.
- ↑ "Flavocytochrome P450 BM3 and the origin of CYP102 fusion species". Biochemical Society Transactions 34 (Pt 6): 1173–7. December 2006. doi:10.1042/BST0341173. PMID 17073779.
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