The active-site residue Tyr-175 in human glyoxalase II contributes to binding of glutathione derivatives

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1481, Issue 2, 2000, Pages 344-348

  Ridderström, Marianne ^a   Jemth, Per ^a   Cameron, Alexander D ^a   Mannervik, Bengt ^a  

^a UPPSALA UNIVERSITY   (Sweden)

Author keywords

Active site; Catalysis; Glutathione; Glyoxalase II; Site directed mutagenesis

Indexed keywords

GLUTATHIONE DERIVATIVE; GLYOXALASE; HYDROXYACYLGLUTATHIONE HYDROLASE; PHENYLALANINE; TYROSINE;

AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME BINDING; ENZYME KINETICS; ENZYME STRUCTURE; FLUORESCENCE; HYDROGEN BOND; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS;

BINDING SITES; CATALYSIS; GLUTATHIONE; HUMAN; KINETICS; MODELS, MOLECULAR; MOLECULAR STRUCTURE; MUTAGENESIS, SITE-DIRECTED; MUTATION; PHENYLALANINE; SPECTROMETRY, FLUORESCENCE; SUPPORT, NON-U.S. GOV'T; THIOLESTER HYDROLASES; TYROSINE;

EID: 0034730564     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(00)00178-3     Document Type: Article

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