Structure and activity of DmmA, a marine haloalkane dehalogenase

Protein Sci. 2012 Feb;21(2):239-48. doi: 10.1002/pro.2009. Epub 2012 Jan 4.

Abstract

DmmA is a haloalkane dehalogenase (HLD) identified and characterized from the metagenomic DNA of a marine microbial consortium. Dehalogenase activity was detected with 1,3-dibromopropane as substrate, with steady-state kinetic parameters typical of HLDs (K(m) = 0.24 ± 0.05 mM, k(cat) = 2.4 ± 0.1 s(-1) ). The 2.2-Å crystal structure of DmmA revealed a fold and active site similar to other HLDs, but with a substantially larger active site binding pocket, suggestive of an ability to act on bulky substrates. This enhanced cavity was shown to accept a range of linear and cyclic substrates, suggesting that DmmA will contribute to the expanding industrial applications of HLDs.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Aquatic Organisms / chemistry
  • Aquatic Organisms / enzymology*
  • Binding Sites
  • Crystallography, X-Ray
  • Cyanobacteria / chemistry
  • Cyanobacteria / enzymology
  • Cyanobacteria / metabolism
  • Enzyme Activation
  • Hydrolases / chemistry*
  • Hydrolases / metabolism*
  • Kinetics
  • Models, Biological
  • Models, Molecular
  • Protein Multimerization / physiology
  • Protein Structure, Quaternary
  • Protein Structure, Secondary
  • Substrate Specificity

Substances

  • Hydrolases
  • haloalkane dehalogenase