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- W1976304874 abstract "Abstract cis,cis-Muconate cycloisomerase (cis,cis-muconate lactonizing enzyme, EC 5.5.1.1.) was purified in crystalline form from Pseudomonas putida. Ultracentrifugation studies, as well as gel filtration chromatography and electrophoresis, indicate that the enzyme is an oligomeric protein of molecular weight 252,000 (s20,w 12.20 × 10−13 s), which is built of six homologous protomers of molecular weight 42,000. Studies of enzyme crystals and enzyme molecules in the electron microscope suggest that the cis,cis-muconate cycloisomerase is a hexamer in which the six protomers are arranged in a dihedral point-group symmetry 32 (D3). Each protomer has a diameter of 42.5Aand six protomers are associated in a structure with a trigonal antiprismatic geometry (a hexamer D3 octahedron). This model could account for the dimensions most frequently observed by negative staining of the enzyme in solution. A model for the three-dimensional structure of enzyme crystals in which each hexameric enzyme molecule is surrounded by eight neighbouring enzyme molecules, is described." @default.
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- W1976304874 date "1974-11-01" @default.
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- W1976304874 title "Molecular properties of cis,cis-muconate cycloisomerase from Pseudomonas putida" @default.
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- W1976304874 doi "https://doi.org/10.1016/0022-2836(74)90042-4" @default.
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