PMID:12883870
| Citation |
Awano, N, Wada, M, Kohdoh, A, Oikawa, T, Takagi, H and Nakamori, S (2003) Effect of cysteine desulfhydrase gene disruption on L-cysteine overproduction in Escherichia coli. Appl. Microbiol. Biotechnol. 62:239-43 |
|---|---|
| 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. |
| Links |
PubMed Online version:10.1007/s00253-003-1262-2 |
| Keywords |
Base Sequence; Cystathionine gamma-Lyase/genetics; Cystathionine gamma-Lyase/metabolism; Cysteine/biosynthesis; DNA, Bacterial/genetics; Enzyme Induction; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli/metabolism; Gene Targeting; Genes, Bacterial; Lyases/biosynthesis; Lyases/genetics; Mutagenesis, Insertional; Tryptophanase/biosynthesis; Tryptophanase/genetics |
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