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- W1974262311 abstract "γ-Glutamyl transpeptidase has been purified about one-hundredfold from acetone powder of housefly (Musca domestica) larvae. The enzyme catalyses the synthesis of γ-glutamylphenylalanine (γ-glu-phe), a dipeptide found in large amounts in the larva of this species. Synthesis is via a classic γ-glutamyl transpeptidation in which the γ-glutamyl residue of γ-glutamylcysteinylglycine (glutathione) is transferred to phenylalanine. Many of the common α-l-amino-acids are also acceptors of the γ-glutamyl residue in vitro, resulting in γ-glutamyl-amino-acid formation. In vivo, however, only γ-glu-phe has been observed to date. Remarkable changes occurred in the amount of γ-glutamyl transpeptidase activity (units per insect or units per mg. protein) at the end of the larval period. Activity doubled at the formation of the puparium, increased a further 50 per cent within the next 1.5–2 hours to its peak level, and then fell abruptly to an almost undetectable level within the subsequent 24 hours. Peak activity coincided with the rapid disappearance of γ-glu-phe during the early stages of sclerotization of the puparium. It is suggested that γ-glu-phe and γ-glutamyl transpeptidase form part of a system of enzymes and their reaction products which constitute a ‘γ-glutamyl cycle’ for the transport of phenylalanine across certain cell membranes in this insect. The cycle appears to operate incompletely during larval growth, resulting in the formation of a pool of γ-glu-phe, while operating completely at puparium formation, resulting in utilization of the pool for sclerotization." @default.
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- W1974262311 date "1971-12-01" @default.
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- W1974262311 title "γ-Glutamyl transpeptidase catalyses the synthesis of γ-glutamylphenylalanine in the larva of the housefly Musca domestica" @default.
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- W1974262311 doi "https://doi.org/10.1016/0020-1790(71)90010-2" @default.
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