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

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

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

Affiliation

Gourley DG; Division of Biochemistry and Molecular Biology, Institute of Biomedical and Life Sciences, University of Glasgow, Scotland, UK.

Nat Struct Biol ; 6(6): 521-5, 1999 Jun.

Article in En | MEDLINE | ID: mdl-10360352

Subject(s)

Hydro-Lyases/chemistry; Hydro-Lyases/metabolism; Mycobacterium tuberculosis/enzymology; Salmonella typhi/enzymology; Binding Sites; Borohydrides/metabolism; Catalysis; Crystallization; Crystallography, X-Ray; Dimerization; Drug Design; Enzyme Inhibitors; Hydro-Lyases/antagonists & inhibitors; Hydro-Lyases/classification; Models, Molecular; Molecular Sequence Data; Protein Folding; Protein Structure, Secondary; Shikimic Acid/metabolism; Structure-Activity Relationship

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Collection: 01-internacional Database: MEDLINE Main subject: Salmonella typhi / Hydro-Lyases / Mycobacterium tuberculosis Language: En Journal: Nat Struct Biol Journal subject: BIOLOGIA MOLECULAR Year: 1999 Document type: Article Affiliation country: United kingdom

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