Biochemical characterization of haloalkane dehalogenases DrbA and DmbC, Representatives of a Novel Subfamily

Appl Environ Microbiol. 2009 Aug;75(15):5157-60. doi: 10.1128/AEM.00199-09. Epub 2009 Jun 5.

Abstract

This study focuses on two representatives of experimentally uncharacterized haloalkane dehalogenases from the subfamily HLD-III. We report biochemical characterization of the expression products of haloalkane dehalogenase genes drbA from Rhodopirellula baltica SH1 and dmbC from Mycobacterium bovis 5033/66. The DrbA and DmbC enzymes show highly oligomeric structures and very low activities with typical substrates of haloalkane dehalogenases.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacteria / enzymology*
  • Circular Dichroism
  • DNA, Bacterial / chemistry
  • DNA, Bacterial / genetics
  • Hydrolases / chemistry
  • Hydrolases / genetics
  • Hydrolases / isolation & purification*
  • Hydrolases / metabolism*
  • Molecular Sequence Data
  • Mycobacterium bovis / enzymology
  • Protein Multimerization
  • Protein Structure, Tertiary
  • Sequence Analysis, DNA
  • Substrate Specificity

Substances

  • DNA, Bacterial
  • Hydrolases
  • haloalkane dehalogenase

Associated data

  • GENBANK/AM696288
  • GENBANK/AM696289