Rational evolution of a medium chain-specific cytochrome P-450 BM-3 variant

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1545, Issue 1-2, 2001, Pages 114-121

  Li, Qing Shan ^a,b   Schwaneberg, Ulrich ^a   Fischer, Markus ^a   Schmitt, Jutta ^a   Pleiss, Jürgen ^a   Lutz Wahl, Sabine ^a   Schmid, Rolf D ^a  

^a UNIVERSITY OF STUTTGART   (Germany)

^b KYOTO UNIVERSITY   (Japan)

Author keywords

Cytochrome P 450; Mutagenesis; Rational evolution

Indexed keywords

CARBOXYLIC ACID DERIVATIVE; CYTOCHROME P450 BM3; CYTOCHROME P450 ISOENZYME; MUTANT PROTEIN; OMEGA 4 NITROPHENOXYCARBOXYLIC ACID DERIVATIVE; OMEGA 4 NITROPHENOXYDECANOIC ACID; OMEGA 4 NITROPHENOXYDODECANOIC ACID; UNCLASSIFIED DRUG;

ARTICLE; BACILLUS MEGATERIUM; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME STRUCTURE; HYDROXYLATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN VARIANT; SITE DIRECTED MUTAGENESIS;

BACILLUS MEGATERIUM; BACTERIAL PROTEINS; CARBOXYLIC ACIDS; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; CYTOCHROME P-450 ENZYME SYSTEM; DRUG DESIGN; EVOLUTION, MOLECULAR; MIXED FUNCTION OXYGENASES; MODELS, MOLECULAR; MOLECULAR STRUCTURE; MUTAGENESIS, SITE-DIRECTED; POLYMERASE CHAIN REACTION; SUBSTRATE SPECIFICITY;

BACILLUS MEGATERIUM;

EID: 0035830723     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(00)00268-5     Document Type: Article

References (16)

1. Fatty acid monooxygenation by cytochrome P-450 BM-3
2. The highly stereoselective oxidation of polyunsaturated fatty acids by cytochrome P-450 BM-3
3. An active site substitution, F87V, converts cytochrome P-450 BM-3 into a regio- and stereoselective (14S,15R)-arachidonic acid epoxygenase
4. Production of chiral hydroxy long chain fatty acids by whole cell biocatalysis of pentadecanoic acid with an E. coli recombinant containing cytochrome P-450 BM-3 monooxygenase
5. Directed evolution of enzyme catalysts
6. Rapid evolution of a protein in vitro by DNA shuffling
7. Highlight: Directed evolution of enzymes
8. The Protein Data Bank: A computer-based archival file for macromolecular structures
9. The structure of the cytochrome P-450 BM-3 haem domain complexed
10. The catalytic mechanism of cytochrome P-450 BM-3 involves a 6 Å movement of the bound substrate on reduction
11. Crystal structure of hemoprotein domain of P-450 BM-3, a prototype for microsomal P-450's
12. A continuous spectrophotometric assay for P-450 BM-3, a fatty acid hydroxylating enzyme, and its mutant F87A
13. A single mutation in cytochrome P-450 BM-3 changes substrate orientation in a catalytic intermediate and the regiospecificity of hydroxylation
14. P-450 monooxygenase in biotechnology. I. Single-step, large-scale purification method for cytochrome P-450 BM-3 by anion-exchange chromatography
15. Directed evolution of a fungal peroxidase