Acyl transfer mechanisms of tissue transglutaminase
| Autor: | Amina Mulani, Kim Y.P. Apperley, Jeffrey W. Keillor, Christopher M. Clouthier, Abdullah Akbar |
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| Rok vydání: | 2014 |
| Předmět: |
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Molecular Protein Conformation Stereochemistry Tissue transglutaminase Acylation Biochemistry Substrate Specificity Hydrolysis Residue (chemistry) GTP-Binding Proteins Drug Discovery Animals Humans Protein Glutamine gamma Glutamyltransferase 2 Deamidation Molecular Biology chemistry.chemical_classification Transglutaminases biology Chemistry Organic Chemistry Enzyme biology.protein Amine gas treating |
| Zdroj: | Bioorganic Chemistry. 57:186-197 |
| ISSN: | 0045-2068 |
| DOI: | 10.1016/j.bioorg.2014.06.003 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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