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 β-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.
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Acknowledgements.
We wish to thank Dr. Winfried Boos for providing the E. coli EZ5, Dr. Isabelle Saint-Girons for providing the pIP29, and Drs. Hiroko Ikushiro and Hiroyuki Kagamiyama for providing the E. coli MD55 and pUC118-tnaA. This work was supported in part by a grant-in-aid for Scientific Research from the Ministry of Education, Science, Sports and Culture of Japan (No. 09660100 to S.N.) and by a grant-in-aid from Ajinomoto Co., Inc.
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Awano, N., Wada, M., Kohdoh, A. et al. Effect of cysteine desulfhydrase gene disruption on l-cysteine overproduction in Escherichia coli . Appl Microbiol Biotechnol 62, 239–243 (2003). https://doi.org/10.1007/s00253-003-1262-2
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DOI: https://doi.org/10.1007/s00253-003-1262-2