STRUCTURAL DOMAINS OF P450-CONTAINING MONOOXYGENASE SYSTEMS

被引：63
作者：
DEGTYARENKO, KN
机构：
[1] INT CTR GENET ENGN & BIOTECHNOL, I-34012 TRIESTE, ITALY
[2] INST BIOMED CHEM, MOSCOW 119832, RUSSIA
来源：
PROTEIN ENGINEERING | 1995年 / 8卷 / 08期
关键词：
CYTOCHROME B(5); FERREDOXIN-NADP(+) REDUCTASE; FLAVODOXIN; IRON-SULFUR PROTEINS; NITRIC OXIDE SYNTHASE; NITRIC OXIDE REDUCTASE; P450-CONTAINING MONOOXYGENASE SYSTEMS; REDOX DOMAINS;
D O I：
10.1093/protein/8.8.737
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
All known P450-containing monooxygenase systems share common structural and functional domain architecture, Apart from P450 itself, these systems can comprise several fundamentally different protein components or domains, all of which are shared by other multicomponent/multidomain enzyme systems with various functions: FAD flavoprotein or domain, FMN domain, Fe2S2 ferredoxin, Fe3S4 ferredoxin, and cytochrome b(5). Either FMN domain, ferredoxins or cytochrome b(5) serve as the electron transport intermediate between the FAD domain and P450. The molecular evolution of both P450-containing systems and of each particular component does not follow phylogeny in general, Gene fusion and horizontal gene transfer events can lead to the appearance of novel redox chains in the same manner that artificial chimeric proteins can be constructed by humans, Recent studies using genetic and protein engineering techniques to investigate the separate domains and their interaction are described.
引用
收藏
页码：737 / 747
页数：11
相关论文
共 118 条
[81]   CRYSTAL-STRUCTURE OF HEMOPROTEIN DOMAIN OF P450BM-3, A PROTOTYPE FOR MICROSOMAL P450S [J].
RAVICHANDRAN, KG ;
BODDUPALLI, SS ;
HASEMANN, CA ;
PETERSON, JA ;
DEISENHOFER, J .
SCIENCE, 1993, 261 (5122) :731-736
[82]   PARTICULAR ABILITY OF LIVER P450S3A TO CATALYZE THE OXIDATION OF N(OMEGA)-HYDROXYARGININE TO CITRULLINE AND NITROGEN-OXIDES AND OCCURRENCE IN NO SYNTHASES OF A SEQUENCE VERY SIMILAR TO THE HEME-BINDING SEQUENCE IN P450S [J].
RENAUD, JP ;
BOUCHER, JL ;
VADON, S ;
DELAFORGE, M ;
MANSUY, D .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1993, 192 (01) :53-60
[83]   COMPARISON OF THE CONSTRUCTION OF A 3-D MODEL FOR HUMAN THROMBOXANE SYNTHASE USING P450CAM AND BM-3 AS TEMPLATES - IMPLICATIONS FOR THE SUBSTRATE-BINDING POCKET [J].
RUAN, KH ;
MILFELD, K ;
KULMACZ, RJ ;
WU, KK .
PROTEIN ENGINEERING, 1994, 7 (11) :1345-1351
[84]  
RUETTINGER RT, 1989, J BIOL CHEM, V264, P10987
[85]  
RUNNEGAR B, 1984, J MOL EVOL, V21, P33, DOI 10.1007/BF02100625
[86]  
SAKAKI T, 1992, J BIOL CHEM, V267, P16497
[87]   KINETIC-STUDIES ON A GENETICALLY-ENGINEERED FUSED ENZYME BETWEEN RAT CYTOCHROME P4501A1 AND YEAST NADPH-P450 REDUCTASE [J].
SAKAKI, T ;
KOMINAMI, S ;
TAKEMORI, S ;
OHKAWA, H ;
AKIYOSHISHIBATA, M ;
YABUSAKI, Y .
BIOCHEMISTRY, 1994, 33 (16) :4933-4939
[88]   CYTOCHROME-OXIDASE EVOLVED BY TINKERING WITH DENITRIFICATION ENZYMES [J].
SARASTE, M ;
CASTRESANA, J .
FEBS LETTERS, 1994, 341 (01) :1-4
[89]   STRUCTURE OF THE DETOXIFICATION CATALYST MERCURIC ION REDUCTASE FROM BACILLUS SP STRAIN-RC607 [J].
SCHIERING, N ;
KABSCH, W ;
MOORE, MJ ;
DISTEFANO, MD ;
WALSH, CT ;
PAI, EF .
NATURE, 1991, 352 (6331) :168-172
[90]   GENE DUPLICATION IN GLUTATHIONE-REDUCTASE [J].
SCHULZ, GE .
JOURNAL OF MOLECULAR BIOLOGY, 1980, 138 (02) :335-347
3456789101112