|
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 |
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