The two types of 3-dehydroquinase have distinct structures but catalyze the same overall reaction

Nature Structural Biology

Volumn 6, Issue 6, 1999, Pages 521-525

  Gourley, D G ^a   Shrive, A K ^a   Polikarpov, I ^a   Krell, T ^a   Coggins, J R ^a   Hawkins, A R ^a   Isaacs, N W ^a   Sawyer, L ^a  

^a UNIVERSITY OF EDINBURGH   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

3 DEHYDROQUINATE DEHYDRATASE; AROMATIC AMINO ACID; FOLIC ACID; SHIKIMIC ACID; UBIQUINONE;

ARTICLE; CATALYSIS; CHEMICAL REACTION KINETICS; CONTROLLED STUDY; ENZYME INHIBITION; ENZYME KINETICS; ENZYME STRUCTURE; NONHUMAN; PRIORITY JOURNAL;

BINDING SITES; BOROHYDRIDES; CATALYSIS; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; DRUG DESIGN; ENZYME INHIBITORS; HYDRO-LYASES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MYCOBACTERIUM TUBERCULOSIS; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SALMONELLA TYPHI; SHIKIMIC ACID; STRUCTURE-ACTIVITY RELATIONSHIP;

ANIMALIA;

EID: 0032979147     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/9287     Document Type: Article

References (40)