type	Journal Article
authors	Awano N, Wada M, Kohdoh A, Oikawa T, Takagi H, Nakamori S.
title	Effect of cysteine desulfhydrase gene disruption on L-cysteine overproduction in Escherichia coli
journal	Appl Microbiol Biotechnol
Activity	4.1.99.1
sel	selected
ui	12883870
year	(2003)
volume	62
number	2
pages	239-43
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.
last changed	2008/01/22 18:28