SCOPUS 정보 검색 플랫폼

Volumn 40, Issue 34, 2001, Pages 10054-10062

Evolution of enzymatic activities in the enolase superfamily: Identification of the general acid catalyst in the active site of D-glucarate dehydratase from Escherichia coli

(4) Gulick, A M a Hubbard, B K b,c Gerlt, J A c Rayment, I a

a UNIVERSITY OF WISCONSIN MADISON (United States)

b UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN (United States)

c HARVARD MEDICAL SCHOOL (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ENZYMATIC ACTIVITIES;

CATALYSIS; CATALYSTS; DEHYDRATION; ESCHERICHIA COLI; MUTAGENESIS; PLASTICITY; STRUCTURAL ANALYSIS;

ENZYMES;

AMINO ACID; ASPARAGINE DERIVATIVE; ASPARTIC ACID DERIVATIVE; DEXTRO GLUCARATE DEHYDRATASE; ENOLASE; HISTIDINE DERIVATIVE; LYSINE DERIVATIVE; UNCLASSIFIED DRUG;

ARTICLE; CATALYST; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ESCHERICHIA COLI; KINETICS; MUTAGENESIS; NONHUMAN; PLASTICITY; PRIORITY JOURNAL; PROTEIN STRUCTURE; STEREOSPECIFICITY; STRUCTURE ANALYSIS;

AMINO ACID SUBSTITUTION; BINDING SITES; CATALYSIS; COMPUTER SIMULATION; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; HYDRO-LYASES; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PHOSPHOPYRUVATE HYDRATASE; PROTEIN STRUCTURE, SECONDARY; PROTEIN SUBUNITS; RECOMBINANT PROTEINS;

EID: 0035964183 PISSN: 00062960 EISSN: None Source Type: Journal
DOI: 10.1021/bi010733b Document Type: Article

Times cited : (25)

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