Gamma-glutamyltranspeptidase, but not YwrD, is important in utilization of extracellular glutathione as a sulfur source in Bacillus subtilis

Hiromichi Minami; Hideyuki Suzuki; Hidehiko Kumagai

doi:10.1128/JB.186.4.1213-1214.2004

Gamma-glutamyltranspeptidase, but not YwrD, is important in utilization of extracellular glutathione as a sulfur source in Bacillus subtilis

J Bacteriol. 2004 Feb;186(4):1213-4. doi: 10.1128/JB.186.4.1213-1214.2004.

Authors

Hiromichi Minami¹, Hideyuki Suzuki, Hidehiko Kumagai

Affiliation

¹ Division of Integrated Life Science, Graduate School of Biostudies, Kyoto University, Kitashirakawa, Sakyo-ku, Kyoto 606-8502, Japan.

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Bacillus subtilis / enzymology*
Bacillus subtilis / growth & development
Bacterial Proteins / physiology*
Culture Media
Glutathione / metabolism*
Sulfur / metabolism*
gamma-Glutamyltransferase / physiology*

Substances

Bacterial Proteins
Culture Media
Sulfur
gamma-Glutamyltransferase
Glutathione