P450 BM3: the very model of a modern flavocytochrome.
Flavocytochrome P450 BM3 is a bacterial P450 system in which a fatty acid hydroxylase P450 is fused to a mammalian-like diflavin NADPH-P450 reductase in a single polypeptide. The enzyme is soluble (unlike mammalian P450 redox systems) and its fusion arrangement affords it the highest catalytic activity of any P450 mono-oxygenase. This article discusses the fundamental properties of P450 BM3 and how progress with this model P450 has affected our comprehension of P450 systems in general.
Munro
Andrew W
AW
Department Biochemistry, University of Leicester, The Adrian Building, University Road, Leicester LE1 7RH, UK. awm9@le.ac.uk
Leys
David G
DG
McLean
Kirsty J
KJ
Marshall
Ker R
KR
Ost
Tobias W B
TW
Daff
Simon
S
Miles
Caroline S
CS
Chapman
Stephen K
SK
Lysek
Dominikus A
DA
Moser
Christopher C
CC
Page
Christopher C
CC
Dutton
P Leslie
PL
D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism*; D001665:Binding Sites; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry* / Q000378:metabolism*; D004579:Electron Transport / Q000502:physiology*; D006899:Mixed Function Oxygenases / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D005810:Multigene Family; D009251:NADPH-Ferrihemoprotein Reductase; D010084:Oxidation-Reduction; D011487:Protein Conformation; D017434:Protein Structure, Tertiary
D001426:Bacterial Proteins; D003577:Cytochrome P-450 Enzyme System; D006899:Mixed Function Oxygenases; D009251:NADPH-Ferrihemoprotein Reductase; C052423:flavocytochrome P450 BM3 monoxygenases