Relationships between Substrate Promiscuity and Chiral Selectivity of Esterases from Phylogenetically and Environmentally Diverse Microorganisms

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  • Cristina Coscolín
    Institute of Catalysis, Consejo Superior de Investigaciones Científicas (CSIC), Madrid
  • Mónica Martínez-Martínez
    Institute of Catalysis
  • Jennifer Chow
    Universität Hamburg
  • Rafael Bargiela
    Institute of Catalysis, Consejo Superior de Investigaciones Científicas (CSIC), Madrid
  • Antonio García-Moyano
    Center for Applied Biotechnology, Bergen
  • Gro E.K. Bjerga
    Center for Applied Biotechnology, Bergen
  • Alexander Bollinger
    Heinrich-Heine-Universität , Dusseldorf
  • Runar Stokke
    Center for Applied Biotechnology, Bergen
  • Ida H. Steen
    Center for Applied Biotechnology, Bergen
  • Olga Golyshina
  • Michail M. Yakimov
    Institute for Coastal Marine Environment
  • Karl-Erich Jaeger
    Bremen University
  • Alexander F. Yakunin
    University of Toronto, Canada
  • Wolfgang R. Streit
    Universität Hamburg
  • Peter Golyshin
  • Manuel Ferrer
    Institute of Catalysis, Consejo Superior de Investigaciones Científicas (CSIC), Madrid
Substrate specificity and selectivity of a biocatalyst are determined by the protein sequence and structure of its active site. Finding versatile biocatalysts acting against multiple substrates while at the same time being chiral selective is of interest for the pharmaceutical and chemical industry. However, the relationships between these two properties in natural microbial enzymes remain underexplored. Here, we performed an experimental analysis of substrate promiscuity and chiral selectivity in a set of 145 purified esterases from phylogenetically and environmentally diverse microorganisms, which were assayed against 96 diverse esters, 20 of which were enantiomers. Our results revealed a negative correlation between substrate promiscuity and chiral selectivity in the evaluated enzymes. Esterases displaying prominent substrate promiscuity and large catalytic environments are characterized by low chiral selectivity, a feature that has limited commercial value. Although a low level of substrate promiscuity does not guarantee high chiral selectivity, the probability that esterases with smaller active sites possess chiral selectivity factors of interest for industry (>25) is significantly higher than for promiscuous enzymes. Together, the present study unambiguously demonstrates that promiscuous and selective esterases appear to be rare in nature and that substrate promiscuity can be used as an indicator of the chiral selectivity level of esterases, and vice versa.
Original languageEnglish
Article number10
JournalCatalysts
Volume8
Issue number1
DOIs
StatePublished - 5 Jan 2018
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