Gamma-glutamyltranspeptidase, but not YwrD, is important in utilization of extracellular glutathione as a sulfur source in Bacillus subtilis.
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.
Minami
Hiromichi
H
Division of Integrated Life Science, Graduate School of Biostudies, Kyoto University, Kitashirakawa, Sakyo-ku, Kyoto 606-8502, Japan.
Suzuki
Hideyuki
H
Kumagai
Hidehiko
H
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*
D001426:Bacterial Proteins; D003470:Culture Media; D013455:Sulfur; D005723:gamma-Glutamyltransferase; D005978:Glutathione