title: Gamma-glutamyltranspeptidase, but not YwrD, is important in utilization of extracellular glutathione as a sulfur source in Bacillus subtilis.
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.
authors.affiliation: Division of Integrated Life Science, Graduate School of Biostudies, Kyoto University, Kitashirakawa, Sakyo-ku, Kyoto 606-8502, Japan.
authors.forename: Hiromichi
authors.initials: H
authors.lastname: Minami
authors.forename: Hideyuki
authors.initials: H
authors.lastname: Suzuki
authors.forename: Hidehiko
authors.initials: H
authors.lastname: Kumagai
mesh_terms: D001412:Bacillus subtilis / Q000201:enzymology* / Q000254:growth & development; D001426:Bacterial Proteins / Q000502:physiology*; D003470:Culture Media; D005978:Glutathione / Q000378:metabolism*; D013455:Sulfur / Q000378:metabolism*; D005723:gamma-Glutamyltransferase / Q000502:physiology*
chemical_list: D001426:Bacterial Proteins; D003470:Culture Media; D013455:Sulfur; D005723:gamma-Glutamyltransferase; D005978:Glutathione