High resolution X-ray structures of different metal-substituted forms of phosphotriesterase from Pseudomonas diminuta.

Benning, M M; Shim, H; Raushel, F M; Holden, H M

Benning, M M; Shim, H; Raushel, F M; Holden, H M.

Affiliation

Benning MM; Department of Biochemistry, University of Wisconsin, Madison, Wisconsin 53706, USA.

Biochemistry ; 40(9): 2712-22, 2001 Mar 06.

Article in En | MEDLINE | ID: mdl-11258882

Subject(s)

Esterases/chemistry; Metals/chemistry; Pseudomonas/enzymology; Aryldialkylphosphatase; Binding Sites; Cadmium/chemistry; Catalysis; Cations, Divalent/chemistry; Crystallography, X-Ray; Dimerization; Manganese/chemistry; Models, Molecular; Protein Structure, Secondary; Substrate Specificity; Zinc/chemistry

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Collection: 01-internacional Database: MEDLINE Main subject: Pseudomonas / Esterases / Metals Language: En Journal: Biochemistry Year: 2001 Document type: Article Affiliation country: United States Country of publication: United States

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