The effect of cysteine mutations on recombinant deacetoxycephalosporin C synthase from S-clavuligerus

被引：25

作者：

Lee, HJ

Lloyd, MD

Harlos, K

Schofield, CJ

机构：

[1] Oxford Ctr Mol Sci, Oxford OX1 3QY, England

[2] Dyson Perrins Lab, Oxford OX1 3QY, England

[3] Natl Def Med Ctr, Dept Biochem, Taipei 10764, Taiwan

[4] Oxford Ctr Mol Sci, Oxford OX1 3QU, England

[5] Mol Biophys Lab, Oxford OX1 3QU, England

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2000年 / 267卷 / 01期

基金：

英国医学研究理事会; 英国工程与自然科学研究理事会; 英国生物技术与生命科学研究理事会;

关键词：

altered substrate specificity; cephem antibiotic biosynthesis; cysteine mutants; iron(II); 2-oxoglutarate oxygenase; penicillin expansion;

D O I：

10.1006/bbrc.1999.1957

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Cysteines 100, 155, and 197 of recombinant deacetoxycephalosporin C synthase were mutated to alanine residues. The C100A mutant had properties similar to those of the wild-type enzyme, but mutation of Cys-155 and Cys-197 reduced enzyme activity with penicillin N and penicillin G to different extents. (C) 2000 Academic Press.

引用

页码：445 / 448

页数：4

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