Cytochromes P450 A Success Story

Genome Biology

Volumn 1, Issue 6, 2000, Pages

  Werck Reichhart, Daniele ^a   Feyereisen, René ^b  

^a CNRS   (France)

^b CEMAGREF   (France)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 33746683848     PISSN: 14656906     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (39)

1. Nelson DR, Koymans L Kamataki T, Stegeman JJ, Feyereisen R, Waxman DJ, Waterman MR, Gotoh O, Coon MJ, Estabrook RW, et al.:P4SO superfamily:update on new sequences, gene mapping, accession numbers and nomenclature:PharmacogenetJcs 1996,6:1-42. This paper defines the rules for P450 gene nomenclature, comments on some general characteristics of the P450 gene superfamilly. and gives a list (with references) of P450 genes identified in various organisms.
2. David Nelson's Homepage [h:tp://drnelson.utmem.edu/CytochromeP4SO.html] David Nelson keeps an update of P450 sequences characterized in all organisms and is also the 'P450 nomenclature committee', the person to contact to obtain a name for a new P450 sequence. Nelson also provides a simple introductory lecture on mammalian P450 enzymes and on all their physiological and other functions.
3. Nelson DR:Cytochrome P4SO and the individuality of species. Aral Biochem Biophys 1999, 369:1-10. This paper defines the clans in P450 classification and gives some examples. In addition to evolutionary considerations, it comments on new P450 genes and functions recently discovered and on P450 polymorphism and its impact on drug metabolism.
4. Ingelman-Sundberg M, Daly AK, Oscarson M, Nebert D:Human cytochrome P450 (CYP) gene:recommandations for the nomenclature of alleles. Pharmacogenetics 2000, 10:91-93. This paper and the related website [6] give rules and examples for the nomenclature of P450 alleles.
5. Home Page of the Human Cytochrome P4SO (CYP) Allele Nomenclature Committee [http://www.imm.ki.se/CYPalleles/] An update of the knowledge on allelic variants of the human genes; also provides instructions on the submission of new variants.
6. Frey M, Chôme:P, Glawischnig E, Stettner C, Grün S, Winklmair A, Eisenreich W, Bacher A, Meeley R B, Briggs SB, et ai:Analysis of a chemical plant defense mechanism in grasses. Science 1997, 277:696-699. The first analysis of a P450 gene cluster in plants (maize). Provides evidence that four evolutionary related P450 genes, belonging to same sub-family and clustered on the same chromosome, catalyze four successive steps in a single pathway.
7. Directory of P450-containing systems [http://www.icgeb.trieste.it/-p450srv/] Lists P450 and related genes. More information on P450 structure, ligands, domain structure, electron donors and useful links on human alleles, drug metabolism, commercially available forms; also contains references.
8. The P4SO site at the University of Arizona [http://ag.arizona.edu/p450/]
9. A site with a list, annotation and a physical map of Drosophi/a and A. thaliana P450s.
10. Rozman D, Stromstedt M, Tsui LC, Scherer SW, Waterman MR:Structure and mapping of the human lanosterol I4ccdemethylase gene (CYP5I) encoding the cytochrome P4SO involved in cholesterol biosynthesis; comparison of exon/intron organization with other mammalian and fungal CYP genes. Genom/cs 1996, 38:371-381. Provides a detailed analysis of a human P450 gene structure and comparative analysis of P450 gene structures in mammals and fungi.
11. Paquette SM, Bak S, Feyereisen R:Intron-exon organization and phylogeny in a large superfamily, the paralogous cytochrome P4SO genes of Arabidopsis thaliana. DNA Cell Biol 2000, 19:307-317. Provides a detailed analysis of the P450 gene family in A. thaliana:gene mapping, phylogeny and intron-exon organization.
12. Tijet N, Helvig C, Feyereisen R:The cytochrome P4SO gene superfamily in Drosophila melanogaster. annotation, intronexon organization and phylogeny. Gene 2000, in press. A complete report on the microsomal and mitochondrial P450s of the fruit fly, their gene structures and their distribution in the genome.
13. Chappie C:Molecular genetics analysis of plant cytochrome P450-dependent monooxygenases. Ann Rev Plant Physio/ Mol Biol 1998,49:311-343. Provides some basic information on P450 characteristics and nomenclature:gives a list of plant P450 genes and mutants already isolated and their functions.
14. Gotoh O:Divergent structures of Caenorhobd/t/î elegans cytochrome P4SO genes suggest the frequent loss and gain of introns during the evolution of nematodes. Mol β/o/ Evo/ 1998, 15:1447-1459. An extensive study of gene structure in the nematode, with a thorough discussion of the process of intron gain and loss in the P450 superfamily.
15. Graham SE, Peterson JA:How similar are P450s and what can their differences teach us. Arch βiophys β/ocfiem 1999, 369:24-29. A recent overview of the available data on P450 three-dimensional structure, comparison of the different crystallized structures in view of substrate specificity and redox partners of the different forms.
16. Gotoh O:Substrate recognition sites in cytochrome P450 family 2 (CYP2) protein inferred from comparative analyses of amino acid and coding nucleotide sequences. J Biol Chem 1992,267:83-90. The reference paper defining the hyper-variable substrate recognition sites (SRSs).
17. Williams PA, Cosme J, Sridhar V, Johnson E, McRee DE:Mammalian microsomal cytochrome P4SO monooxygenase:structural adaptations for membrane binding and functional diversity. Mol Cell 2000, 5:121-131. First structural report on a microsomal enzyme:describes similarities and difference with the soluble forms.
18. Julian A ('Bill') Peterson's home page [http://p450terp.swmed.edu/Bills_fo!der/billhorne.htm] An easy access to didactic pictures illustrating P450 interaction with the P450-reductase and active-site structure.
19. The Scripps Institute P450 protein site [http://metallo.scripps.edu/PROMlSE/P450.html] Information on prosthetic group, different P450 types, reaction catalyzed, P450 enzyme, motif and alignment databases, three-dimensional (3D) structure databases and structural references.
20. Poulos TL, Finzel B C, Gunsalus 1C, Wagner GC, Kraut J:The 2.6-A crystal structure of Pseudomonas putirfa cytochrome P-450./ Biol Chem I98S. 260:16122-16130. The first high-resolution structure of a bacterial soluble (class I) P450.
21. Schlichting I, Berendzen J, Chu K, Stock AM, Maves SA, Benson DE, Sweet RM, Ringe D, Petsko GA, Sugar SG:The catalytic pathway of cytochrome P450cam at atomic resolution. Science 2000, 287:1615-1622. The most recent update on the 3D structure of class I bacterial enzymes:includes the structure of one-electron-reduced forms and of the activated oxygen complex. Two forms of activated oxygen are detected in the crystal, confirming the biochemical data of [35J.
22. Ravichandran KG, Boddupalli SS, Hasemann CA, Peterson JA, Deisendorfer J:Crystal structure of hemoprotein domain of P450BM-3, a prototype for microsomal FMSO's. Science 1993, 261:731-736. The first description of the 3D structure of a class II enzyme. Until the coordinates of the mammalian CYP2C5 become available, probably in the next year, this serves as a reference for the eukaryotic membranebound enzymes.
23. Li H, Poulos Tu The structure of the cytochrome P450BM-3 haem domain complexée] with the fatty acid substrate, palmitoleic acid. Nat Struct Bio) 1997, 4:140-146. A very interesting description of the class II enzyme Crystallized with its substrate. A model for fatty-acid-metabolizing P450s in all kingdoms, providing the first detailed picture of substrate-induced conformational changes in a P450.
24. Park SY, Shimizu H, Adachi S, Nakagawa A, Tanaka I, Nakahara K, Shoun H, Obayashi E, Nakamura H, lizuka T, Shiro Y:Crystal structure of nitric oxide reductase from denitrifying fungus Fusarium oxysporum. Nat Struct Biol 1997, 10:827-832. First description of the 3D structure of a class IV enzyme. Provides evidence of significant differences in proton delivery and access of NADH to the active site.
25. Hasler JA, Estabrook R, Murray M, Pikuleva I, Waterman M, Capdevila J, Holla V, Helvig C, Falck JR, Farrell G, et al:Human cytochromes P4SO. Mol Aspects Med 1999, 20:1 -137. A very complete overview of P450 roles in human normal physiology, pathology and drug metabolism.
26. Feyereisen R:Insect cytochrome P4SO enzymes. Anna Rev Entomo/ 1999,44:507-533. Provides a review of the physiological functions of insect P450 as well as the role and regulation of P450 in insecticide metabolism, insecticide resistance, and the adaptation to plant chemicals.
27. Kahn R, Durst F:Function and evolution of plant cytochrome P450. Recent Adv Phytocfiem 2000, 34:151-189.
28. The most recent review on the role of P450 enzymes in the biosynthesis of plant natural compounds. Also comments on plant P450 evolution and techniques useful for plant P450 gene isolation.
29. Gonzalez FJ, Kimura S:Role of gene knockout mice in understanding the mechanisms of chemical toxicity and carcinogenesis. Cancer Lett 1999, 143:199-204. Provides a description of the gene disruption technology in the mouse and its application for the study of three P450 genes involved in xenobiotic metabolism.
30. Werck-Reichhart D, Hehn H, Didierjean L:Cytochromes P450 for engineering herbicide tolerance. Trends Plant Sei 2000, 5:116-123. Reviews available data in the metabolism of exogenous compounds, in particular herbicides, in higher plants and the impact of altered metabolism on weed resistance.
31. Waxnnan DJ:P450 gene induction by structurally diverse xenochemicals:central role of nuclear receptors CAR, PXR, and PPAR. Arch Biodiem Biophys 1999, 369:11-23. Summarizes recent progress in nuclear receptor driven regulation of mammalian P450s by xenochemicals. The expression of different P450 families is driven by specific nuclear receptors of the family NRI activated by exogenous and endogenous ligands.
32. Honkakoski P, Negishi M:Regulation of cytochrome P4SO genes by nuclear receptors, βiochem J 2000, 347:321-337. Gives an overview of the nuclear receptors involved in P450 gene regulation, of their respective role in endobiotic and xenobiotic metabolism, with emphasis on the potential impact of exogenous compounds on cellular homeostasis.
33. Mansuy D:The great diversity of reactions catalyzed by cytochrome P450. Comp Biochem Physio) Part C 1998, 121:5-14. A good simplified overview on the diversity and mechanism of reaction catalyzed by P450 enzymes.
34. Klingenberg M:Pigments of rat liver microsomes. Arch Biochem Biophys 1958,75:376-386. first description of a pigment absorbing at 450 nm when reduced in mammalian liver microsomes.
35. Omura T, Sato R:The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature, j B/olChem 1964,239:2370-2378 Demonstration of the hemoprotein nature of the pigment absorbing at 450 nm:gives the extinction coefficient used for all P450 quantifications..
36. Newcomb M, Shen R, Choi S-Y, Toy PH, Hollenberg PF, Vaz ADN, Coon MJ:Cytochrome P450-catalyzed hydroxylation of mechanistic probes that distinguish between radical and cations, evidence for cationic but not radical intermediates. J Am Chem Soc 2000, 122:2677-2686. The most recent update on P450 catalytical mechanism. Provides evidence of the existence of two activated oxygen forms (iron-oxo and hydroperoxo-iron) for the same enzymes, both forms producing different products with mechanistic probes. Also gives evidence that reaction occurs in both cases by direct insertion.
37. Jefcoate C R:Measurement of substrate and inhibitor binding to microsomal cytochrome P450 by optical difference spectroscopy. Methods Enzymol 1978, 52:258-279. A reference paper that provides the basis for ligand-binding detection by spectrophotometry.
38. Fred K. Friedman's Home Page [http://rex.nci.nih.gov/RESEARCH/basic/lm/fkf.htm] The place to see a model of P450 insertion in a membrane.
39. Williams PA, Cosme J, Sridhar V, Johnson EF, McRee DE:Microsomal cytochrome P450 2C5:comparison to microbial P450s and unique features.] Inorg Biochem 2000, 81:183-190, More pictures to illustrate the differences between microbial and membrane-bound proteins.