Identification and functional analysis of Escherichia coli cysteine desulfhydrases

被引:133
作者
Awano, N
Wada, M
Mori, H
Nakamori, S
Takagi, H
机构
[1] Fukui Prefectural Univ, Dept Biosci, Matsuoka, Fukui 9101195, Japan
[2] Nara Inst Sci & Technol, Res & Educ Ctr Genet Informat, Ikoma 6300101, Japan
关键词
D O I
10.1128/AEM.71.7.4149-4152.2005
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, three additional proteins having L-cysteine desulfhydrase activity were identified as O-acetylserine sulfhydrylase-A, O-acetylserine sulfhydrylase-B, and MalY protein, in addition to tryptophanase and cystathionine beta-lyase, which have been reported previously. The gene disruption for each protein was significantly effective for overproduction Of L-cysteine and L-cystine. Growth phenotype and transcriptional analyses suggest that tryptophanase contributes primarily to L-cysteine degradation.
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收藏
页码:4149 / 4152
页数:4
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