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γ‐Glutamylcysteinylserine — A New Homologue of Glutathione in Plants of the Family Poaceae *
Author(s) -
Klapheck S.,
Chrost B.,
Starke J.,
Zimmermann H.
Publication year - 1992
Publication title -
botanica acta
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.871
H-Index - 87
eISSN - 1438-8677
pISSN - 0932-8629
DOI - 10.1111/j.1438-8677.1992.tb00284.x
Subject(s) - tripeptide , glutathione , biochemistry , buthionine sulfoximine , glutathione reductase , biology , poaceae , amino acid , incubation , chemistry , enzyme , botany , glutathione peroxidase
In addition to glutathione (γ‐GluCysGly), many species of the family Poaceae have another tripeptide which has the amino acid sequence γ‐GluCysSer. This thiol was isolated from etiolated leaves of wheat ( Triticum aestivum L. cv. Star). Its structure was elucidated by quantitative amino acid analysis after total hydrolysis and by partial hydrolysis with carboxypeptidase A and γ‐glutamyltranspeptidase. The content of γ‐GluCysSer in the leaves of T. aestivum is increased by incubation with sulfate and is severely diminished by incubation with buthionine sulfoximine, a specific inhibitor of γ‐glutamylcysteine synthetase. Oxidized γ‐GluCysSer is reduced by yeast glutathione reductase with a rate somewhat lower than for glutathione, but the new tripeptide is not a substrate of glutathione‐S‐transferase from equine liver. Besides homoglutathione (γ‐GluCysßAla), a tripeptide found in plants of the order Fabales, the tripeptide γ‐GluCysSer is the second homologue of glutathione detected in plants.