The PatB protein of Bacillus subtilis is a C-S-lyase

被引：45

作者：

Auger, S ^{[1
]}

Gomez, MP ^{[1
]}

Danchin, A ^{[1
]}

Martin-Verstraete, I ^{[1
]}

机构：

[1] Inst Pasteur, CNRS, URA 2171, Unite Genet Genom Bacteriens, F-75724 Paris, France

来源：

BIOCHIMIE | 2005年 / 87卷 / 02期

关键词：

sulfur metabolism; cystathionine beta-lyase; cysteine desulfhydrase; methionine biosynthesis;

D O I：

10.1016/j.biochi.2004.09.007

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：

The PatB protein of Bacillus subtilis had both cystathionine P-lyase and cysteine desulfhydrase activities in vitro. The apparent K-m value of the PatB protein for cystathionine was threefold higher than that of the MetC protein, the previously characterized cystathionine P-lyase of B. subtilis. In the presence of cystathionine as sole Sulfur source, the patB gene present on a multicopy plasmid restored the growth of a metC mutant. In addition. the patB metC double mutant was unable to grow in the presence of sulfate or cystine while the patB or metC single Mutants grew similarly to the wild-type strains in the presence of the same sulfur sources. In a metC mutant, the PatB protein can replace the MetC enzyme in the methionine biosynthetic pathway. (c) 2004 Elsevier SAS. All rights reserved.

引用

页码：231 / 238

页数：8

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