Difference between revisions of "Cytochrome P450 family"
(→Relevant reviews) |
|||
| Line 14: | Line 14: | ||
<pubmed> 15122913 </pubmed> | <pubmed> 15122913 </pubmed> | ||
==Relevant reviews== | ==Relevant reviews== | ||
| − | <pubmed> 10462435 19559718 20302567 20177889 20132846 20068028 20064075 8042852 15832443 2064373 23632015 23632016 17023115 </pubmed> | + | <pubmed> 10462435 19559718 20302567 20177889 20132846 20068028 20064075 8042852 15832443 2064373 23632015 23632016 17023115 23632017 </pubmed> |
Revision as of 13:30, 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
Courtney M Krest, Elizabeth L Onderko, Timothy H Yosca, Julio C Calixto, Richard F Karp, Jovan Livada, Jonathan Rittle, Michael T Green
Reactive intermediates in cytochrome p450 catalysis.
J Biol Chem: 2013, 288(24);17074-81
[PubMed:23632017]
[WorldCat.org]
[DOI]
(I p)
F Peter Guengerich, Andrew W Munro
Unusual cytochrome p450 enzymes and reactions.
J Biol Chem: 2013, 288(24);17065-73
[PubMed:23632016]
[WorldCat.org]
[DOI]
(I p)
F Peter Guengerich
New trends in cytochrome p450 research at the half-century mark.
J Biol Chem: 2013, 288(24);17063-4
[PubMed:23632015]
[WorldCat.org]
[DOI]
(I p)
Peter Hlavica, Michael Lehnerer
Oxidative biotransformation of fatty acids by cytochromes P450: predicted key structural elements orchestrating substrate specificity, regioselectivity and catalytic efficiency.
Curr Drug Metab: 2010, 11(1);85-104
[PubMed:20302567]
[WorldCat.org]
[DOI]
(I p)
Toshiki Furuya, Kuniki Kino
Genome mining approach for the discovery of novel cytochrome P450 biocatalysts.
Appl Microbiol Biotechnol: 2010, 86(4);991-1002
[PubMed:20177889]
[WorldCat.org]
[DOI]
(I p)
D E Torres Pazmiño, M Winkler, A Glieder, M W Fraaije
Monooxygenases as biocatalysts: Classification, mechanistic aspects and biotechnological applications.
J Biotechnol: 2010, 146(1-2);9-24
[PubMed:20132846]
[WorldCat.org]
[DOI]
(I p)
Tsuneo Omura
Structural diversity of cytochrome P450 enzyme system.
J Biochem: 2010, 147(3);297-306
[PubMed:20068028]
[WorldCat.org]
[DOI]
(I p)
Santosh Kumar
Engineering cytochrome P450 biocatalysts for biotechnology, medicine and bioremediation.
Expert Opin Drug Metab Toxicol: 2010, 6(2);115-31
[PubMed:20064075]
[WorldCat.org]
[DOI]
(I p)
Toshiki Furuya, Daisuke Shibata, Kuniki Kino
Phylogenetic analysis of Bacillus P450 monooxygenases and evaluation of their activity towards steroids.
Steroids: 2009, 74(12);906-12
[PubMed:19559718]
[WorldCat.org]
[DOI]
(I p)
Andrew W Munro, Hazel M Girvan, Kirsty J McLean
Cytochrome P450--redox partner fusion enzymes.
Biochim Biophys Acta: 2007, 1770(3);345-59
[PubMed:17023115]
[WorldCat.org]
[DOI]
(P p)
Minor J Coon
Cytochrome P450: nature's most versatile biological catalyst.
Annu Rev Pharmacol Toxicol: 2005, 45;1-25
[PubMed:15832443]
[WorldCat.org]
[DOI]
(P p)
D R Nelson
Cytochrome P450 and the individuality of species.
Arch Biochem Biophys: 1999, 369(1);1-10
[PubMed:10462435]
[WorldCat.org]
[DOI]
(P p)
K Oguri, H Yamada, H Yoshimura
Regiochemistry of cytochrome P450 isozymes.
Annu Rev Pharmacol Toxicol: 1994, 34;251-79
[PubMed:8042852]
[WorldCat.org]
[DOI]
(P p)
A J Fulco
P450BM-3 and other inducible bacterial P450 cytochromes: biochemistry and regulation.
Annu Rev Pharmacol Toxicol: 1991, 31;177-203
[PubMed:2064373]
[WorldCat.org]
[DOI]
(P p)
