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

Abstract:

: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 beta-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.

authors

Awano N,Wada M,Kohdoh A,Oikawa T,Takagi H,Nakamori S

doi

10.1007/s00253-003-1262-2

subject

Has Abstract

pub_date

2003-08-01 00:00:00

pages

239-43

issue

2-3

eissn

0175-7598

issn

1432-0614

journal_volume

62

pub_type

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