• Open Access

Isolation and initial characterization of a novel type of Baeyer–Villiger monooxygenase activity from a marine microorganism

Authors

  • Andrew Willetts,

    Corresponding author
    1. Plymouth Marine Laboratory, Prospect Place, The Hoe, Plymouth PL1 3DH, UK
    2. Curnow Consultancies, Trewithen House, Ashton, Helston TR13 9PQ, UK
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  • Ian Joint,

    1. Marine Biological Association of the UK, The Laboratory, Citadel Hill, Plymouth PL1 2PB, UK
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  • Jack A. Gilbert,

    1. Argonne National Laboratory, Bldg 202, Biosciences B373, 9700 South Cass Ave, Argonne, IL 60439, USA
    2. Institute of Genomics and Systems Biology, Argonne National Laboratory and University of Chicago, IL 60437, USA
    3. Department of Ecology and Evolution, University of Chicago, 5640 South Ellis Avenue, Chicago, IL 60637, USA
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  • William Trimble,

    1. Institute of Genomics and Systems Biology, Argonne National Laboratory and University of Chicago, IL 60437, USA
    2. Department of Ecology and Evolution, University of Chicago, 5640 South Ellis Avenue, Chicago, IL 60637, USA
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  • Martin Mühling

    1. Plymouth Marine Laboratory, Prospect Place, The Hoe, Plymouth PL1 3DH, UK
    2. Institute of Biological Sciences, TU Bergakademie Freiberg, Leipziger Str. 29, 09599 Freiberg, Germany
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E-mail andrewj.willetts@btconnect.com; Tel. (+44) 1392 851304; Fax (+44) 1392 851304.

Summary

A novel type of Baeyer–Villiger monooxygenase (BVMO) has been found in a marine strain of Stenotrophomonas maltophila strain PML168 that was isolated from a temperate intertidal zone. The enzyme is able to use NADH as the source of reducing power necessary to accept the atom of diatomic oxygen not incorporated into the oxyfunctionalized substrate. Growth studies have establish that the enzyme is inducible, appears to serve a catabolic role, and is specifically induced by one or more unidentified components of seawater as well as various anthropogenic xenobiotic compounds. A blast search of the primary sequence of the enzyme, recovered from the genomic sequence of the isolate, has placed this atypical BVMO in the context of the several hundred known members of the flavoprotein monooxygenase superfamily. A particular feature of this BVMO lies in its truncated C-terminal domain, which results in a relatively small protein (357 amino acids; 38.4 kDa). In addition, metagenomic screening has been conducted on DNA recovered from an extensive range of marine environmental samples to gauge the relative abundance and distribution of similar enzymes within the global marine microbial community. Although low, abundance was detected in samples from many marine provinces, confirming the potential for biodiscovery in marine microorganisms.

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