Stereoselective hydroxylation of an achiral cyclopentanecarboxylic acid derivative using engineered P450s BM-3.
Substrate engineered, achiral carboxylic acid derivative was biohydroxylated with various mutants of cytochrome P450 BM-3 to give two out of the four possible diastereoisomers in high de and ee. The BM-3 mutants exhibit up to 9200 total turnovers for hydroxylation of the engineered substrate, which without the protecting group is not transformed by this enzyme.
Münzer
Dieter F
DF
Institut für Organische Chemie der Technischen Universität Graz, Austria.
Meinhold
Peter
P
Peters
Matthew W
MW
Feichtenhofer
Sabine
S
Griengl
Herfried
H
Arnold
Frances H
FH
Glieder
Anton
A
de Raadt
Anna
A
D001426:Bacterial Proteins / Q000737:chemistry*; D002264:Carboxylic Acids / Q000138:chemical synthesis* / Q000737:chemistry; D003517:Cyclopentanes / Q000737:chemistry*; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry*; D006900:Hydroxylation; D006899:Mixed Function Oxygenases / Q000737:chemistry*; D008968:Molecular Conformation; D009251:NADPH-Ferrihemoprotein Reductase; D015202:Protein Engineering / Q000379:methods*; D013237:Stereoisomerism; D013379:Substrate Specificity
D001426:Bacterial Proteins; D002264:Carboxylic Acids; D003517:Cyclopentanes; D003577:Cytochrome P-450 Enzyme System; D006899:Mixed Function Oxygenases; D009251:NADPH-Ferrihemoprotein Reductase; C052423:flavocytochrome P450 BM3 monoxygenases