A highly active single-mutation variant of P450BM3 (CYP102A1).
The power of proline: Bold amino acid substitutions in sensitive protein regions are frequently unproductive, while more subtle mutations can be sufficient to bring about dramatic changes. But introducing proline at the residue next to the sulfur ligand in P450(BM3) (CYP102A1) has the unexpected and desirable effect of enhancing the activity of this fatty acid hydroxylase with a broad range of non-natural substrates, as illustrated by the figure.
Whitehouse
Christopher J C
CJ
Department of Chemistry, University of Oxford, Inorganic Chemistry Laboratory, South Parks Road, Oxford, UK.
Bell
Stephen G
SG
Yang
Wen
W
Yorke
Jake A
JA
Blanford
Christopher F
CF
Strong
Anthony J F
AJ
Morse
Edward J
EJ
Bartlam
Mark
M
Rao
Zihe
Z
Wong
Luet-Lok
LL
D019943:Amino Acid Substitution; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D005227:Fatty Acids / Q000378:metabolism; D007700:Kinetics; D009154:Mutation; D009251:NADPH-Ferrihemoprotein Reductase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
D001426:Bacterial Proteins; D005227:Fatty Acids; D011994:Recombinant Proteins; D003577:Cytochrome P-450 Enzyme System; D009251:NADPH-Ferrihemoprotein Reductase; C052423:flavocytochrome P450 BM3 monoxygenases