| Identification and characterization of gamma-glutamylamine cyclotransferase, an enzyme responsible for gamma-glutamyl-epsilon-lysine catabolism. | |
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MedLine Citation:
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PMID: 20110353 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Gamma-glutamylamine cyclotransferase (GGACT) is an enzyme that converts gamma-glutamylamines to free amines and 5-oxoproline. GGACT shows high activity toward gamma-glutamyl-epsilon-lysine, derived from the breakdown of fibrin and other proteins cross-linked by transglutaminases. The enzyme adopts the newly identified cyclotransferase fold, observed in gamma-glutamylcyclotransferase (GGCT), an enzyme with activity toward gamma-glutamyl-alpha-amino acids (Oakley, A. J., Yamada, T., Liu, D., Coggan, M., Clark, A. G., and Board, P. G. (2008) J. Biol. Chem. 283, 22031-22042). Despite the absence of significant sequence identity, several residues are conserved in the active sites of GGCT and GGACT, including a putative catalytic acid/base residue (GGACT Glu(82)). The structure of GGACT in complex with the reaction product 5-oxoproline provides evidence for a common catalytic mechanism in both enzymes. The proposed mechanism, combined with the three-dimensional structures, also explains the different substrate specificities of these enzymes. Despite significant sequence divergence, there are at least three subfamilies in prokaryotes and eukaryotes that have conserved the GGCT fold and GGCT enzymatic activity. |
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Authors:
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Aaron J Oakley; Marjorie Coggan; Philip G Board |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2010-01-28 |
Journal Detail:
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Title: The Journal of biological chemistry Volume: 285 ISSN: 1083-351X ISO Abbreviation: J. Biol. Chem. Publication Date: 2010 Mar |
Date Detail:
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Created Date: 2010-03-22 Completed Date: 2010-04-26 Revised Date: 2011-07-27 |
Medline Journal Info:
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Nlm Unique ID: 2985121R Medline TA: J Biol Chem Country: United States |
Other Details:
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Languages: eng Pagination: 9642-8 Citation Subset: IM |
Affiliation:
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Division of Molecular and Health Technologies, Commonwealth Scientific and Industrial Research Organization, Parkville, Victoria 3052, Australia. |
| Data Bank Information | |
Bank Name/Acc. No.:
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PDB/3JUB; 3JUC; 3JUD |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Catalysis Catalytic Domain Cell Line, Tumor Cloning, Molecular Cross-Linking Reagents / chemistry Crystallography, X-Ray / methods Dipeptides / chemistry* Gene Expression Regulation, Enzymologic* Gene Expression Regulation, Neoplastic* Humans Molecular Sequence Data Mutagenesis, Site-Directed Protein Conformation Pyrrolidonecarboxylic Acid / chemistry Sequence Homology, Amino Acid gamma-Glutamylcyclotransferase / chemistry*, genetics* |
| Chemical | |
Reg. No./Substance:
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0/Cross-Linking Reagents; 0/Dipeptides; 17105-15-6/epsilon-(gamma-glutamyl)-lysine; 98-79-3/Pyrrolidonecarboxylic Acid; EC 2.3.2.4/gamma-Glutamylcyclotransferase |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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