Critical role of the residue size at position 87 in H2O2-dependent substrate hydroxylation activity and H2O2 inactivation of cytochrome P450BM-3

Biochemical and Biophysical Research Communications

Volumn 280, Issue 5, 2001, Pages 1258-1261

  Li, Qing Shan ^a   Ogawa, Jun ^a   Shimizu, Sakayu ^a  

^a KYOTO UNIVERSITY   (Japan)

Author keywords

Hydrogen peroxide inactivation; P450BM 3; Peroxide supported activity

Indexed keywords

4 NITROPHENOXYDODECANOIC ACID; ALANINE; CYTOCHROME P450 ISOENZYME; CYTOCHROME P450BM 3; FATTY ACID; GLYCINE; HEME; HYDROGEN PEROXIDE; IRON; LAURIC ACID DERIVATIVE; OXYGEN; PHENYLALANINE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; UNCLASSIFIED DRUG;

ARTICLE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME INACTIVATION; ENZYME STABILITY; HYDROXYLATION; NONHUMAN; OXIDATION; PRIORITY JOURNAL;

EID: 0034815974     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1006/bbrc.2001.4261     Document Type: Article

References (16)

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2. Characterization of a catalytically self-sufficient 119,000-Dalton cytochrome P450 monoxygenase induced by barbiturates in Bacillus megaterium
3. Fatty acid monooxygenation by cytochrome P450BM-3
4. An active site substitution, F87V, converts cytochrome P450BM-3 into a regio- and stereoselective (14S, 15R)-arachidonic acid epoxygenase
5. Molecular modelling of CYP1 family enzymes CYP1A1, CYP1A2, CYP1A6 and CYP1B1 based on sequence homology with CYP102
6. Thr268 in substrate binding and catalysis in P4350BM-3
7. Directed evolution of the fatty acid hydroxylase P450BM-3 into an indole-hydroxylating catalyst
8. A continuous spectrophotometric assay for P450BM-3, a fatty acid hydroxylating enzyme, and its mutant F87A
9. The carbon monoxide-binding pigment of liver microsomes: I evidence for its hemoprotein nature
10. A single mutation in cytochrome P450BM3 changes substrate orientation in a catalytic intermediate and the regiospecificity of hydroxylation
11. 2 with peroxy compounds
12. Reactions and significance of cytochrome P450 enzymes
13. The structure of the cytochrome p450BM-3 haem domain complexed with the fatty acid structure, palmitoleic acid
14. Crystal structure of hemoprotein domain of P450BM-3, a prototype for microsomal P450's
15. The catalytic mechanism of cytochrome P450BM3 involves a 6 A movement of the bound substrate on reduction
16. Laboratory evolution of peroxide-mediated cytochrome P450 hydroxylation