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 {EC number|2.3.2.13}. Bonds ...
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http://en.wikipedia.org/wiki/Transglutaminase
<enzyme> An important extracellular enzyme that catalyses the formation of an amide bond between side chain glutamine and side chain lysine residues in proteins with the elimination of ammonia. The linkage is stable and plays an important role in many extracellular assembly processes. ... (18 Nov 1997) ...
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http://www.encyclo.co.uk/local/20973
(trans″gloo-tam´in-ās) the activated form of protransglutaminase, which forms stabilizing covalent bonds within fibrin strands; called also factor XIIIa (the activated form of factor XIII).
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http://www.encyclo.co.uk/local/21001
An important extracellular enzyme that catalyses the formation of an amide bond between side-chain glutamine and side-chain lysine residues in proteins with the elimination of ammonia. The linkage is stable and plays an important role in many extracellular assembly processes.
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http://www.encyclo.co.uk/visitor-contributions.php
Type: Term Pronunciation: tranz′glū-ta′min-ās Definitions: 1. A group of enzymes that catalyze the calcium-dependent acyl transfer reaction in which the amide moiety of peptide-bound glutaminyl residues serve as acyl donor; a specific transglutaminase covalently cross-links fibrin molecules between glutamine and the ε-ami...
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http://www.medilexicon.com/medicaldictionary.php?t=93283
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