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Literature summary for 3.4.19.13 extracted from

  • Minami, H.; Suzuki, H.; Kumagai, H.
    gamma-Glutamyltranspeptidase, but not YwrD, is important in utilization of extracellular glutathione as a sulfur source in Bacillus subtilis (2004), J. Bacteriol., 186, 1213-1214.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Bacillus subtilis P54422
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-
Bacillus subtilis 168 P54422
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glutathione + H2O
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Bacillus subtilis L-cysteinylglycine + L-glutamate
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?
glutathione + H2O
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Bacillus subtilis 168 L-cysteinylglycine + L-glutamate
-
?

General Information

General Information Comment Organism
physiological function enzyme is important in utilizing glutathione as the sole sulfur source in Bacillus subtilis. With glutathione as a sulfur source, the growth of enzyme deletion mutants is dramatically reduced compared to that of the wild type. Findings suggest that extracellular enzyme catalyzes the hydrolysis of the gamma-glutamyl linkage of exogenous glutathione and then cysteinylglycine is utilized as a sulfur source in the cell Bacillus subtilis