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Crystal structure of human glyoxalase .1. Evidence for gene duplication and 3D domain swapping
Uppsala University.
Uppsala University.
Uppsala University.
Uppsala University.
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1997 (English)In: EMBO JOURNAL, ISSN 0261-4189, Vol. 16, no 12, 3386-3395 p.Article in journal (Other scientific) Published
Abstract [en]

The zinc metalloenzyme glyoxalase I catalyses the glutathione-dependent inactivation of toxic methylglyoxal. The structure of the dimeric human enzyme in complex with S-benzyl-glutathione has been determined by multiple isomorphous replacement (MIR) and r

Place, publisher, year, edition, pages
OXFORD UNIV PRESS , 1997. Vol. 16, no 12, 3386-3395 p.
Keyword [en]
gene duplication; glutathione; glyoxalase I; 3D domain swapping; zinc coordination; ACTIVE-SITE; TRIOSEPHOSPHATE ISOMERASE; PSEUDOMONAS-PUTIDA; ALIGNMENT; CLONING; METAL; ZINC; REFINEMENT; DATABASE; FAMILIES
Identifiers
URN: urn:nbn:se:uu:diva-79613OAI: oai:DiVA.org:uu-79613DiVA: diva2:107526
Note
Addresses: UPPSALA UNIV, BIOMED CTR, DEPT MOL BIOL, S-75124 UPPSALA, SWEDEN. UNIV UPPSALA, CTR BIOMED, DEPT BIOCHEM, S-75123 UPPSALA, SWEDEN.Available from: 2008-10-17 Created: 2008-10-17 Last updated: 2011-01-15

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