Structure of dehydroquinate synthase reveals an active site capable of multistep catalysis

Nature

Volumn 394, Issue 6690, 1998, Pages 299-302

  Carpenter, Elisabeth P ^a   Hawkins, Alastair R ^b   Frost, John W ^c   Brown, Katherine A ^d  

^a NATIONAL INSTITUTE FOR MEDICAL RESEARCH   (United Kingdom)

^b NEWCASTLE UNIVERSITY   (United Kingdom)

^c MICHIGAN STATE UNIVERSITY   (United States)

^d IMPERIAL COLLEGE LONDON   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

3 DEHYDROQUINATE SYNTHASE; ALCOHOL DEHYDROGENASE; ANTIFUNGAL AGENT; ANTIINFECTIVE AGENT; NICOTINAMIDE ADENINE DINUCLEOTIDE; POLYPEPTIDE; SHIKIMIC ACID; SYNTHETASE;

AMINO TERMINAL SEQUENCE; ARTICLE; ASPERGILLUS NIDULANS; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME STRUCTURE; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING;

ALCOHOL OXIDOREDUCTASES; ASPERGILLUS NIDULANS; BINDING SITES; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; HYDRO-LYASES; LYASES; MODELS, MOLECULAR; MULTIENZYME COMPLEXES; OXIDATION-REDUCTION; PHOSPHORUS-OXYGEN LYASES; PHOSPHOTRANSFERASES (ALCOHOL GROUP ACCEPTOR); PROTEIN CONFORMATION; TRANSFERASES;

ASPERGILLUS; EMERICELLA NIDULANS; EUKARYOTA; MAMMALIA;

EID: 0032537722     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/28431     Document Type: Article

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