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Applied and Environmental Microbiology, July 2005, p. 4149-4152, Vol. 71, No. 7
0099-2240/05/$08.00+0     doi:10.1128/AEM.71.7.4149-4152.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

SHORT REPORT

Identification and Functional Analysis of Escherichia coli Cysteine Desulfhydrases

Naoki Awano,1 Masaru Wada,1,{dagger} Hirotada Mori,2 Shigeru Nakamori,1 and Hiroshi Takagi1*

Department of Bioscience, Fukui Prefectural University, 4-1-1 Kenjojima, Matsuoka-cho, Fukui 910-1195,1 Research and Education Center for Genetic Information, Nara Institute of Science and Technology, Ikoma 630-0101, Japan2

Received 9 October 2004/ Accepted 2 February 2005

In Escherichia coli, three additional proteins having L-cysteine desulfhydrase activity were identified as O-acetylserine sulfhydrylase-A, O-acetylserine sulfhydrylase-B, and MalY protein, in addition to tryptophanase and cystathionine ß-lyase, which have been reported previously. The gene disruption for each protein was significantly effective for overproduction of L-cysteine and L-cystine. Growth phenotype and transcriptional analyses suggest that tryptophanase contributes primarily to L-cysteine degradation.

* Corresponding author. Mailing address: Department of Bioscience, Fukui Prefectural University, 4-1-1 Kenjojima, Matsuoka-cho, Fukui 910-1195, Japan. Phone: 81-776-61-6000. Fax: 81-776-61-6015. E-mail: hiro{at}fpu.ac.jp.

{dagger} Present address: Division of Applied Bioscience, Graduate School of Agriculture, Hokkaido University, Sapporo 060-8589, Japan.

Applied and Environmental Microbiology, July 2005, p. 4149-4152, Vol. 71, No. 7
0099-2240/05/$08.00+0     doi:10.1128/AEM.71.7.4149-4152.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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