Effect of cysteine desulfhydrase gene disruption on L-cysteine overproduction in Escherichia coli

被引：58

作者：

Awano, N ^{[1
]}

Wada, M ^{[1
]}

Kohdoh, A ^{[1
]}

Oikawa, T ^{[1
]}

Takagi, H ^{[1
]}

Nakamori, S ^{[1
]}

机构：

[1] Fukui Prefectural Univ, Dept Biosci, Matsuoka, Fukui 9101195, Japan

来源：

APPLIED MICROBIOLOGY AND BIOTECHNOLOGY | 2003年 / 62卷 / 2-3期

关键词：

D O I：

10.1007/s00253-003-1262-2

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

In Escherichia coli, the enzyme called cysteine desulfhydrase (CD), which is responsible for L-cysteine degradation, was investigated by native-PAGE and CD activity staining of crude cell extracts. Analyses with gene-disrupted mutants showed that CD activity resulted from two enzymes: tryptophanase (TNase) encoded by tnaA and cystathionine P-lyase (CBL) encoded by metC. It was also found that TNase synthesis was induced by the presence Of L-Cysteine. The tnaA and metC mutants transformed with the plasmid containing the gene for feedback-insensitive serine acetyltransferase exhibited higher L-Cysteine productivity than the wild-type strain carrying the same plasmid. These results indicated that TNase and CBL did act on L-Cysteine degradation in E. coli cells.

引用

页码：239 / 243

页数：5

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