Thioredoxin motif of Caenorhabditis elegans PDI-3 provides Cys and His catalytic residues for transglutaminase activity

被引：15

作者：

Blaskó, B

Mádi, A

Fésüs, L

机构：

[1] Univ Debrecen, Med & Hlth Sci Ctr, Fac Med, Dept Biochem & Mol Biol, H-4012 Debrecen, Hungary

[2] Univ Debrecen, Hungarian Acad Sci, Signal & Apoptosis Res Grp, H-4012 Debrecen, Hungary

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2003年 / 303卷 / 04期

关键词：

protein disulphide isomerase; transglutaminase; active site; catalytic triad; Caenorhabditis elegans;

D O I：

10.1016/S0006-291X(03)00490-X

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Previous reports have suggested that protein disulfide isomerases (PDIs) have transglutaminase (TGase) activity [1]. The structural basis of this reaction has not been revealed. We demonstrate here that Caenorhabditis elegans PDI-3 can function as a Ca2+-dependent TGase in assays based on modification of protein- and peptide-bound glutamine residues. By site-directed mutagenesis the second cysteine residue of the -CysGlyHisCys- motif in the thioredoxin domain of the enzyme protein was found to be the active site of the transamidation reaction and chemical modification of histidine in their motif blocked TGase activity. (C) 2003 Elsevier Science (USA). All rights reserved.

引用

页码：1142 / 1147

页数：6

共 28 条

[1] Structure of the Rho-activating domain of Escherichia coli cytotoxic necrotizing factor 1 [J].