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Titolo:
Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue
Autore:
Cameron, AD; Ridderstrom, M; Olin, B; Mannervik, B;
Indirizzi:
Uppsala Univ, Ctr Biomed, Dept Mol Biol, S-75124 Uppsala, Sweden Uppsala Univ Uppsala Sweden S-75124 pt Mol Biol, S-75124 Uppsala, Sweden Uppsala Univ, Ctr Biomed, Dept Biochem, S-75123 Uppsala, Sweden Uppsala Univ Uppsala Sweden S-75123 ept Biochem, S-75123 Uppsala, Sweden
Titolo Testata:
STRUCTURE WITH FOLDING & DESIGN
fascicolo: 9, volume: 7, anno: 1999,
pagine: 1067 - 1078
SICI:
0969-2126(19990915)7:9<1067:CSOHGI>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
METALLO-BETA-LACTAMASE; ANGSTROM RESOLUTION; BACILLUS-CEREUS; BACTEROIDES-FRAGILIS; ARABIDOPSIS-THALIANA; ACTIVE-SITE; ZINC; REFINEMENT; INHIBITION; ALIGNMENT;
Keywords:
binuclear zinc site; crystal structure; glyoxalase II; glutathione; thiolesterase;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
57
Recensione:
Indirizzi per estratti:
Indirizzo: Cameron, AD Univ York, Dept Chem, Struct Biol Lab, York YO10 5DD, N Yorkshire, England Univ York York N Yorkshire England YO10 5DD orkshire, England
Citazione:
A.D. Cameron et al., "Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue", STRUCT F D, 7(9), 1999, pp. 1067-1078

Abstract

Background: Glyoxalase II, the second of two enzymes in the glyoxalase system, is a thiolesterase that catalyses the hydrolysis of S-D-lactoylgtutathione to form glutathione and D-lactic acid. Results: The structure of human glyoxalase II was solved initially by single isomorphous replacement with anomalous scattering and refined at a resolution of 1.9 Angstrom. The enzyme consists of two domains. The first domainfolds into a four-layered beta sandwich, similar to that seen in the metallo-beta-lactamases. The second domain is predominantly cc-helical. The active site contains a binuclear zinc-binding site and a substrate-binding siteextending over the domain interface. The model contains acetate and cacodylate in the active site. A second complex was derived from crystals soaked in a solution containing the slow substrate, S-(N-hydroxy-N-bromophenylcarbamoyl)glutathione. This complex was refined at a resolution of 1.46 Angstrom. It contains the added ligand in one molecule of the asymmetric unit and glutathione in the other. Conclusions: The arrangement of ligands around the zinc ions includes a water molecule, presumably in the form of a hydroxide ion, coordinated to both metal ions. This hydroxide ion is situated 2.9 Angstrom from the carbonylcarbon of the substrate in such a position that it could act as the nucleophile during catalysis. The reaction mechanism may also have implications for the action of metallo-beta-lactamases.

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Documento generato il 03/04/20 alle ore 10:56:04