Crystal structure of type I 3-dehydroquinate dehydratase of Aquifex aeolicus suggests closing of active site flap is not essential for enzyme action

Biochemical and Biophysical Research Communications

Volumn 432, Issue 2, 2013, Pages 350-354

  Devi, Aribam Swarmistha ^a   Ebihara, Akio ^b   Kuramitsu, Seiki ^b,c   Yokoyama, Shigeyuki ^d,e   Kumarevel, Thirumananseri ^b   Ponnuraj, Karthe ^a  

^a UNIVERSITY OF MADRAS   (India)

^b RIKEN SPring 8 Center   (Japan)

^c OSAKA UNIVERSITY   (Japan)

^d RIKEN YOKOHAMA INSTITUTE   (Japan)

^e UNIVERSITY OF TOKYO   (Japan)

Author keywords

Antimicrobial; Aquifex aeolicus; Crystal structure; Shikimate pathway; Thermostability; Type I 3 dehydroquinate dehydratase

Indexed keywords

3 DEHYDROQUINATE DEHYDRATASE;

AQUIFEX AEOLICUS; ARTICLE; BIOCATALYSIS; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME STRUCTURE; GENE EXPRESSION; GENE SEQUENCE; HYPERTHERMOPHILIC BACTERIUM; LIGAND BINDING; MOLECULAR CLONING; PRIORITY JOURNAL; PROTEIN STRUCTURE;

BACTERIA; BACTERIAL PROTEINS; CATALYTIC DOMAIN; CLONING, MOLECULAR; CRYSTALLOGRAPHY, X-RAY; HYDRO-LYASES; PROTEIN STRUCTURE, SECONDARY;

AQUIFEX AEOLICUS; BACTERIA (MICROORGANISMS); MAMMALIA;

EID: 84875240254     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2013.01.099     Document Type: Article

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