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    Tytuł:
    Larger active site in an ancestral hydroxynitrile lyase increases catalytically promiscuous esterase activity.
    Autorzy:
    Jones BJ; Department of Biochemistry, Molecular Biology and Biophysics and The Biotechnology Institute, University of Minnesota, Saint Paul, Minnesota, United States of America.
    Evans RL 3rd; Department of Biochemistry, Molecular Biology and Biophysics and The Biotechnology Institute, University of Minnesota, Saint Paul, Minnesota, United States of America.
    Mylrea NJ; Department of Biochemistry, Molecular Biology and Biophysics and The Biotechnology Institute, University of Minnesota, Saint Paul, Minnesota, United States of America.
    Chaudhury D; Department of Biochemistry, Molecular Biology and Biophysics and The Biotechnology Institute, University of Minnesota, Saint Paul, Minnesota, United States of America.
    Luo C; Department of Biochemistry, Molecular Biology and Biophysics and The Biotechnology Institute, University of Minnesota, Saint Paul, Minnesota, United States of America.
    Guan B; Department of Biochemistry, Molecular Biology and Biophysics and The Biotechnology Institute, University of Minnesota, Saint Paul, Minnesota, United States of America.
    Pierce CT; Department of Biochemistry, Molecular Biology and Biophysics and The Biotechnology Institute, University of Minnesota, Saint Paul, Minnesota, United States of America.
    Gordon WR; Department of Biochemistry, Molecular Biology and Biophysics and The Biotechnology Institute, University of Minnesota, Saint Paul, Minnesota, United States of America.
    Wilmot CM; Department of Biochemistry, Molecular Biology and Biophysics and The Biotechnology Institute, University of Minnesota, Saint Paul, Minnesota, United States of America.
    Kazlauskas RJ; Department of Biochemistry, Molecular Biology and Biophysics and The Biotechnology Institute, University of Minnesota, Saint Paul, Minnesota, United States of America.
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    Źródło:
    PloS one [PLoS One] 2020 Jun 30; Vol. 15 (6), pp. e0235341. Date of Electronic Publication: 2020 Jun 30 (Print Publication: 2020).
    Typ publikacji:
    Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.
    MeSH Terms:
    Aldehyde-Lyases/*chemistry
    Aldehyde-Lyases/genetics ; Catalytic Domain ; Crystallography, X-Ray/methods ; Esterases/chemistry ; Esterases/genetics ; Hevea/genetics ; Hevea/metabolism ; Models, Molecular ; Molecular Structure ; Mutagenesis, Site-Directed/methods ; Plant Proteins/genetics ; Protein Folding ; Substrate Specificity ; Nicotiana/genetics ; Nicotiana/metabolism
    Czasopismo naukowe
    Pełny tekst  Link otwiera się w nowym oknie Pełny tekstSzczegóły
    Tytuł:
    Crystal structures reveal metal-binding plasticity at the metallo-β-lactamase active site of PqqB from Pseudomonas putida.
    Autorzy:
    Tu X; Department of Biochemistry, Molecular Biology, and Biophysics, and The Biotechnology Institute, University of Minnesota, St Paul, MN, 55108, USA.
    Latham JA; Departments of Chemistry, and Molecular and Cellular Biology, University of California, Berkeley, CA, 94720, USA.; Department of Chemistry and Biochemistry, University of Denver, Denver, CO, 80208, USA.
    Klema VJ; Department of Biochemistry, Molecular Biology, and Biophysics, and The Biotechnology Institute, University of Minnesota, St Paul, MN, 55108, USA.; Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX, 77555, USA.
    Evans RL 3rd; Department of Biochemistry, Molecular Biology, and Biophysics, and The Biotechnology Institute, University of Minnesota, St Paul, MN, 55108, USA.
    Li C; Department of Biochemistry, Molecular Biology, and Biophysics, and The Biotechnology Institute, University of Minnesota, St Paul, MN, 55108, USA.
    Klinman JP; Departments of Chemistry, and Molecular and Cellular Biology, University of California, Berkeley, CA, 94720, USA.
    Wilmot CM; Department of Biochemistry, Molecular Biology, and Biophysics, and The Biotechnology Institute, University of Minnesota, St Paul, MN, 55108, USA. .
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    Źródło:
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry [J Biol Inorg Chem] 2017 Oct; Vol. 22 (7), pp. 1089-1097. Date of Electronic Publication: 2017 Aug 19.
    Typ publikacji:
    Journal Article
    MeSH Terms:
    Bacterial Proteins/*metabolism
    Metals/*metabolism
    Pseudomonas putida/*enzymology
    beta-Lactamases/*metabolism
    Bacterial Proteins/chemistry ; Binding Sites ; Catalytic Domain ; Crystallography, X-Ray ; Humans ; Metals/chemistry ; Models, Molecular ; PQQ Cofactor/metabolism ; Protein Binding ; Protein Conformation ; Pseudomonas Infections/microbiology ; Pseudomonas putida/chemistry ; Pseudomonas putida/metabolism ; beta-Lactamases/chemistry
    Czasopismo naukowe
    Pełny tekst  Link otwiera się w nowym oknieSzczegóły
      Wyświetlanie 1-2 z 2

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