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Journal of Bacteriology, February 2004, p. 1213-1214, Vol. 186, No. 4
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.4.1213-1214.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

{gamma}-Glutamyltranspeptidase, but Not YwrD, Is Important in Utilization of Extracellular Glutathione as a Sulfur Source in Bacillus subtilis

Hiromichi Minami, Hideyuki Suzuki,* and Hidehiko Kumagai

Division of Integrated Life Science, Graduate School of Biostudies, Kyoto University, Kitashirakawa, Sakyo-ku, Kyoto 606-8502, Japan

Received 28 July 2003/ Accepted 3 November 2003

{gamma}-Glutamyltranspeptidase (EC 2.3.2.2) of Bacillus subtilis, which is an extracellular enzyme, hydrolyzes the {gamma}-glutamyl linkage of glutathione. YwrD, which is homologous to {gamma}-glutamyltranspeptidase, was speculated to have a similar physiological role. It was shown that {gamma}-glutamyltranspeptidase, but not YwrD, is important in utilizing glutathione as the sole sulfur source in Bacillus subtilis.

* Corresponding author. Mailing address: Division of Integrated Life Science, Graduate School of Biostudies, Kyoto University, Kitashirakawa, Sakyo-ku, Kyoto 606-8502, Japan. Phone: 81-75-753-6278. Fax: 81-75-753-6275. E-mail: hideyuki{at}lif.kyoto-u.ac.jp.

Journal of Bacteriology, February 2004, p. 1213-1214, Vol. 186, No. 4
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.4.1213-1214.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Kimura, K., Tran, L.-S. P., Uchida, I., Itoh, Y. (2004). Characterization of Bacillus subtilis {gamma}-glutamyltransferase and its involvement in the degradation of capsule poly-{gamma}-glutamate. Microbiology 150: 4115-4123 [Abstract] [Full Text]  


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