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Appl Environ Microbiol. 2014 Dec;80(23):7303-15. doi: 10.1128/AEM.01985-14. Epub 2014 Sep 19.

Expanding the Halohydrin Dehalogenase Enzyme Family: Identification of Novel Enzymes by Database Mining.

Author information

1
Junior Professorship for Biocatalysis, Institute of Biotechnology, RWTH Aachen University, Aachen, Germany.
2
Enzymicals AG, Greifswald, Germany.
3
Junior Professorship for Biocatalysis, Institute of Biotechnology, RWTH Aachen University, Aachen, Germany a.schallmey@biotec.rwth-aachen.de.

Abstract

Halohydrin dehalogenases are very rare enzymes that are naturally involved in the mineralization of halogenated xenobiotics. Due to their catalytic potential and promiscuity, many biocatalytic reactions have been described that have led to several interesting and industrially important applications. Nevertheless, only a few of these enzymes have been made available through recombinant techniques; hence, it is of general interest to expand the repertoire of these enzymes so as to enable novel biocatalytic applications. After the identification of specific sequence motifs, 37 novel enzyme sequences were readily identified in public sequence databases. All enzymes that could be heterologously expressed also catalyzed typical halohydrin dehalogenase reactions. Phylogenetic inference for enzymes of the halohydrin dehalogenase enzyme family confirmed that all enzymes form a distinct monophyletic clade within the short-chain dehydrogenase/reductase superfamily. In addition, the majority of novel enzymes are substantially different from previously known phylogenetic subtypes. Consequently, four additional phylogenetic subtypes were defined, greatly expanding the halohydrin dehalogenase enzyme family. We show that the enormous wealth of environmental and genome sequences present in public databases can be tapped for in silico identification of very rare but biotechnologically important biocatalysts. Our findings help to readily identify halohydrin dehalogenases in ever-growing sequence databases and, as a consequence, make even more members of this interesting enzyme family available to the scientific and industrial community.

PMID:
25239895
PMCID:
PMC4249193
DOI:
10.1128/AEM.01985-14
[Indexed for MEDLINE]
Free PMC Article

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