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transglutaminase : ウィキペディア英語版 | transglutaminase
A transglutaminase is an enzyme that catalyzes the formation of an isopeptide bond between a free amine group (e.g., protein- or peptide-bound lysine) and the acyl group at the end of the side chain of protein- or peptide-bound glutamine. The reaction also produces a molecule of ammonia. Such an enzyme is classified as . Bonds formed by transglutaminase exhibit high resistance to proteolytic degradation (proteolysis). Transglutaminases were first described in 1959.〔 〕 The exact biochemical activity of transglutaminases was discovered in blood coagulation protein factor XIII in 1968. ==Physiological transglutaminases== Eight transglutaminases have been characterised.
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