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Reaction mechanism of glyoxalase I explored by an X-ray crystallographic analysis of the human enzyme in complex with a transition state analogue
Uppsala University.
Uppsala University.
Uppsala University.
Uppsala University.
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1999 (English)In: BIOCHEMISTRY, ISSN 0006-2960, Vol. 38, no 41, 13480-13490 p.Article in journal (Other scientific) Published
Abstract [en]

The structures of human glyoxalase I in complexes with S-(N-hydroxy-N-p-iodophenylcarbamoyl)glutathione (HIPC-GSH) and S-p-nitrobenzyloxycarbonylglutathione (NBC-GSH) have been determined at 2.0 and 1.72 Angstrom resolution, respectively. HIPC-GSH is a tr

Place, publisher, year, edition, pages
AMER CHEMICAL SOC , 1999. Vol. 38, no 41, 13480-13490 p.
Keyword [en]
ACTIVE-SITE; TRIOSEPHOSPHATE ISOMERASE; SUBSTRATE USAGE; REFINEMENT; SYSTEM; METAL; NMR; DERIVATIVES; INHIBITORS; RESONANCE
Identifiers
URN: urn:nbn:se:uu:diva-84914OAI: oai:DiVA.org:uu-84914DiVA: diva2:112822
Note
Addresses: Cameron AD, Univ York, Dept Chem, Struct Biol Lab, York YO10 5DD, N Yorkshire, England. Uppsala Univ, Ctr Biomed, Dept Biol Mol, S-75124 Uppsala, Sweden. Uppsala Univ, Ctr Biomed, Dept Biochem, S-75124 Uppsala, Sweden. Univ Maryland, Dept ChemAvailable from: 2008-10-17 Created: 2008-10-17 Last updated: 2011-01-14

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