Abstract
Gene Cloning of &gamma-Glutamyltranspeptidase and Its Relationship to Endogenous Formaldehyde in Shiitake Mushroom (<em>Lentinus edodes</em>)
Highlights
Γ-Glutamyltranspeptidase (GGT) is a major enzyme of Glutathione (GSH) homeostasis and is the only peptidase catalyzing hydrolysis of peptide bonds involving a γ-glutamyl residue as well as the removal of γ-glutamyl moiety from glutathione and other related γglutamyl compounds to other amino acids and peptides (Tate and Meister, 1981; Taniguchi and Ikeda, 1998)
From alliums plants, GGT from shiitake mushroom is found as one of key enzymes in the odor formation pathway, where it catalyzes the conversion of lentinic acid to methyl disulfide with the cooperation of S-alkyll-cysteine sulfoxidelyase (C-S lyase) and methyl disulfide is polymerized to cyclic and linear sulfur compounds leading to the specific odor
Characterization of the full-length GGT: The presence of GGT activity has been confirmed from bacteria to mammals and the complete full-length Open Reading Frame (ORF) of GGT has been found in some mammals, plants, bacillus etc
Summary
Γ-Glutamyltranspeptidase (GGT) is a major enzyme of Glutathione (GSH) homeostasis and is the only peptidase catalyzing hydrolysis of peptide bonds involving a γ-glutamyl residue as well as the removal of γ-glutamyl moiety from glutathione and other related γglutamyl compounds to other amino acids and peptides (Tate and Meister, 1981; Taniguchi and Ikeda, 1998). In the present work, we cloned the gene of shiitake GGT by rapid amplification of cDNA ends (RACE). Rapid amplification of cDNA ends (RACE): Total RNA was extracted from maturated fruiting bodies with the TRIzol® reagent (Invitrogen, US) according to the manufacturer’s instructions.
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