کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1355925 | 1500457 | 2014 | 12 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Acyl transfer mechanisms of tissue transglutaminase Acyl transfer mechanisms of tissue transglutaminase](/preview/png/1355925.png)
• Review of detailed mechanisms of tissue transglutaminase.
• Amide hydrolysis and transamidation reactions.
• Catalytic machinery resembles cysteine proteases.
• Activity regulated through large conformational changes.
Tissue transglutaminase (TG2) is a calcium-dependent enzyme that catalyses several acyl transfer reactions. The most biologically relevant of these involve protein-bound Gln residues as an acyl-donor substrate, and either water or a primary amine as an acyl-acceptor substrate. The former leads to deamidation of Gln to Glu, whereas the latter leads to transamidation, typically resulting in protein cross-linking when the amine substrate is a protein-bound Lys residue. In this review, we present an overview of over fifty years of mechanistic studies that have led to our current understanding of TG2-mediated hydrolysis and transamidation.
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Journal: Bioorganic Chemistry - Volume 57, December 2014, Pages 186–197