نتایج جستجو برای: transamidation

تعداد نتایج: 189  

Journal: :The Journal of biological chemistry 2013
Gayathri N Silva Shirin Fatma Ashley M Floyd Frederic Fischer Pitak Chuawong Amanda N Cruz Rachel M Simari Nilesh Joshi Daniel Kern Tamara L Hendrickson

Many bacteria lack genes encoding asparaginyl- and/or glutaminyl-tRNA synthetase and consequently rely on an indirect path for the synthesis of both Asn-tRNA(Asn) and Gln-tRNA(Gln). In some bacteria such as Thermus thermophilus, efficient delivery of misacylated tRNA to the downstream amidotransferase (AdT) is ensured by formation of a stable, tRNA-dependent macromolecular complex called the As...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1997
U L RajBhandary

Aminoacyl-tRNA synthetases play a central role in protein synthesis by covalently linking the correct amino acid to the correct tRNA (1). Each aminoacyl-tRNA is then carried to the ribosome where it interacts with the cognate trinucleotide codon on the mRNA and transfers the amino acid onto a growing polypeptide chain. Work on tRNAs and aminoacyltRNA synthetases from bacteria, fungi, plants, an...

Journal: :Frontiers in bioscience : a journal and virtual library 2006
Evgeny A Zemskov Anna Janiak Jun Hang Anu Waghray Alexey M Belkin

Numerous studies over the last two decades revealed a complexity and multiple functions of tissue transglutaminase (tTG or TG2, EC 2.3.2.13). Besides the ability to catalyze Ca2+-dependent transamidation of proteins and formation of protein polymers via protease-resistant covalent isopeptide bonds, tTG also possesses GTPase enzymatic activity which links this protein to certain intracellular si...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1999
M Sissler C Delorme J Bond S D Ehrlich P Renault C Francklyn

In addition to their essential catalytic role in protein biosynthesis, aminoacyl-tRNA synthetases participate in numerous other functions, including regulation of gene expression and amino acid biosynthesis via transamidation pathways. Herein, we describe a class of aminoacyl-tRNA synthetase-like (HisZ) proteins based on the catalytic core of the contemporary class II histidyl-tRNA synthetase w...

Journal: :Gut 2007
Greg Byrne Fergus Ryan John Jackson Con Feighery Jacinta Kelly

BACKGROUND AND AIMS Tissue transglutaminase (tTG) is an autoantigen in coeliac disease and the related disorder, dermatitis herpetiformis. The detection of autoantibodies directed against tTG is a highly specific marker of coeliac disease; however, it is unclear if there is a role for these autoantibodies in the disease process. The aim of this study was to investigate whether the catalytic tri...

Journal: :FASEB journal : official publication of the Federation of American Societies for Experimental Biology 2002
Francesca Bernassola Massimo Federici Marco Corazzari Alessandro Terrinoni Marta L Hribal Vincenzo De Laurenzi Marco Ranalli Ornella Massa Giorgio Sesti W H Irwin McLean Gennaro Citro Fabrizio Barbetti Gerry Melino

Transglutaminase 2 (TGase 2) is a Ca+2-dependent enzyme that catalyzes both intracellular and extracellular cross-linking reactions by transamidation of specific glutamine residues. TGase 2 is known to be involved in the membrane-mediated events required for glucose-stimulated insulin release from the pancreatic beta cells. Here we show that targeted disruption of TGase 2 impairs glucose-stimul...

Journal: :Frontiers in bioscience : a journal and virtual library 2006
Kapil Mehta Jansina Y Fok Lingegowda S Mangala

Tissue transglutaminase (TG2, EC 2.3.2.13) is a ubiquitous enzyme that catalyzes Ca2+-dependent post-translational modification of proteins by inserting highly stable (epsilon-[gamma-glutamyl] lysine) isopeptide bonds or by conjugating polyamines at selected peptide-bound glutamine residues. The TG2-catalyzed cross-linked products (generally high molecular mass scaffold of proteins) are of grea...

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