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- W1996474085 abstract "L-Glutamine is one of the most abundant amino acids that can be synthesized de novo in most mammalian cells. The glutamine harbors a carboxamido functional group in the c position with a high-energy C–N bond. The protein-bound glutamine residues, unlike glutamate residues, do not undergo glutarimide formation and isoglutamate rearrangements, and the amide moiety of glutamine renders the residue capable of forming c-glutamyl isopeptide cross-links via the incorporation of primary amines from other proteins. Heinrich Waelsch and colleagues [1,2] identified an amine-incorporating activity in liver homogenates, showed that the amines are attached to the c-glutam(in)yl moieties after the release of ammonia, and termed this activity ‘‘transglutaminase.’’ Lorand et al. [3] described a similar catalytic mechanism for plasma coagulation factor XIII and adopted Waelsch s transglutaminase (TGase) nomenclature. Further research has identified TGase activity in many vertebrates, plants, protozoa, and bacteria (recently reviewed in [4,5]). Nine homologous transglutaminase genes have been identified in humans and mice, all except one (erythrocyte band 4.2) code active transglutaminases (TGases 1–7 and factor XIIIa), which are variably expressed in multiple organs and cell types of the organism [6]." @default.
- W1996474085 created "2016-06-24" @default.
- W1996474085 creator A5014742619 @default.
- W1996474085 creator A5028400916 @default.
- W1996474085 creator A5091056693 @default.
- W1996474085 date "2005-07-01" @default.
- W1996474085 modified "2023-10-17" @default.
- W1996474085 title "Tools for the detection and quantitation of protein transglutamination" @default.
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- W1996474085 doi "https://doi.org/10.1016/j.ab.2004.10.015" @default.