Difference between revisions of "Cytochrome P450 family"
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* [[YrhJ]] (CYP102A3) | * [[YrhJ]] (CYP102A3) | ||
| + | == P450 in Bacillus== | ||
| + | <pubmed> 15122913 </pubmed> | ||
==Relevant reviews== | ==Relevant reviews== | ||
| − | <pubmed> 10462435 19559718 20302567 20177889 20132846 20068028 20064075 8042852 15832443 2064373 23632015 23632016 </pubmed> | + | <pubmed> 10462435 19559718 20302567 20177889 20132846 20068028 20064075 8042852 15832443 2064373 23632015 23632016 17023115 </pubmed> |
Revision as of 13:28, 31 July 2013
Contents
- 1 The cytochrome P450 superfamily (officially abbreviated as CYP) is a large and diverse group of enzymes. The function of most CYP enzymes is to catalyze the oxidation of organic substances. The substrates of CYP enzymes include metabolic intermediates such as lipids and steroidal hormones, as well as xenobiotic substances such as drugs and other toxic chemicals
- 2 B. subtilis encodes eight cytochromes P450:
- 3 P450 in Bacillus
- 4 Relevant reviews
The cytochrome P450 superfamily (officially abbreviated as CYP) is a large and diverse group of enzymes. The function of most CYP enzymes is to catalyze the oxidation of organic substances. The substrates of CYP enzymes include metabolic intermediates such as lipids and steroidal hormones, as well as xenobiotic substances such as drugs and other toxic chemicals
B. subtilis encodes eight cytochromes P450:
- BioI (CYP107H1)
- CypA (CYP107J1)
- CypC (CYP152A1)
- CypX (CYP134A1)
- PksS (CYP107K1)
- YetO (CYP102A2)
- YjiB (CYP109B1)
- YrhJ (CYP102A3)
P450 in Bacillus
Mattias C U Gustafsson, Olivier Roitel, Ker R Marshall, Michael A Noble, Stephen K Chapman, Antonio Pessegueiro, Armand J Fulco, Myles R Cheesman, Claes von Wachenfeldt, Andrew W Munro
Expression, purification, and characterization of Bacillus subtilis cytochromes P450 CYP102A2 and CYP102A3: flavocytochrome homologues of P450 BM3 from Bacillus megaterium.
Biochemistry: 2004, 43(18);5474-87
[PubMed:15122913]
[WorldCat.org]
[DOI]
(P p)
Relevant reviews
