3-D structure of a mutant (Asp101 -> Ser) of E.coli alkaline phosphatase with higher catalytic activity |
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| Authors: | Chen, Liqing Neidhart, David Kohlbrenner, William M. Mandecki, Wlodek Bell, Sean Sowadski, Janusz Abad-Zapatero, Cele |
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| Affiliation: | 1Laboratory of Protein Crystallography University of California at San Diego 9500 Gilman Drive, La Jolla, Ca 92093-0654, USA 2Anti-infective Enzymology, University of California at San Diego 9500 Gilman Drive, La Jolla, Ca 92093-0654, USA 3Corporate Molecular Biology, Abbott Laboratories Abbott Park, IL 60064 4Department of Medicine and Biology, University of California at San Diego 9500 Gilman Drive, La Jolla, Ca 92093-0654, USA 5Present address: Department of Biology, Room 16-739, Massachusetts Institute of Technology 77 Massachusetts Avenue, Cambridge, MA 02139, USA 6Present address: Monsanto Corporate Research, BB4K, 700 Chesterfield Village Parkway, Chesterfield, MO 63198, USA |
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| Abstract: | Mutagenesis of the absolutely conserved residue Asp101 of thenon-specific monoesterase alkaline phosphatase (E.C. 3.1.3.1[EC])from E.coli has produced an enzyme with increased kcat. Thecarboxyl group of the Asp101 residue has been proposed to beinvolved in the positioning of Arg166 and the formation of thehelix that contains the active site Ser 102. The crystal structureof the Asp101 |
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