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Volumn 38, Issue 49, 1999, Pages 16187-16194

An asparagine-phenylalanine substitution accounts for catalytic differences between hGSTM3-3 and other human class Mu glutathione S- transferases

(3) Patskovsky, Yury V a Patskovska, Larysa N a Listowsky, Irving a

a ALBERT EINSTEIN COLLEGE OF MEDICINE (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE; CHIMERIC PROTEIN; GLUTATHIONE TRANSFERASE; MUTANT PROTEIN; PHENYLALANINE;

AMINO ACID SUBSTITUTION; ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; ENZYME SUBUNIT; HUMAN; HUMAN CELL; PH; PRIORITY JOURNAL; PROTEIN DOMAIN;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ASPARAGINE; BINDING SITES; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; DINITROCHLOROBENZENE; GLUTATHIONE TRANSFERASE; HUMANS; HYDROGEN-ION CONCENTRATION; KINETICS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PHENYLALANINE; POINT MUTATION; RECOMBINANT FUSION PROTEINS;

EID: 0033534153 PISSN: 00062960 EISSN: None Source Type: Journal
DOI: 10.1021/bi991714t Document Type: Article

Times cited : (19)

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