DspA from Strongylocentrotus purpuratus: The first biochemically characterized haloalkane dehalogenase of non-microbial origin
Language English Country France Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
23939220
DOI
10.1016/j.biochi.2013.07.025
PII: S0300-9084(13)00248-4
Knihovny.cz E-resources
- Keywords
- CD, Catalytic activity, Enantioselectivity, Eukaryotic haloalkane dehalogenase, Gene mining, IPTG, PCA, Principle Component Analysis, Substrate specificity, T(m), circular dichroism, isopropyl β-D-thiogalactopyranoside, melting temperature,
- MeSH
- Circular Dichroism MeSH
- Halogens chemistry MeSH
- Hydrolases chemistry genetics MeSH
- Catalysis MeSH
- Cloning, Molecular MeSH
- Gene Expression Regulation, Enzymologic MeSH
- Amino Acid Sequence genetics MeSH
- Strongylocentrotus purpuratus enzymology genetics MeSH
- Substrate Specificity MeSH
- Carbon chemistry MeSH
- Animals MeSH
- Check Tag
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- haloalkane dehalogenase MeSH Browser
- Halogens MeSH
- Hydrolases MeSH
- Carbon MeSH
Haloalkane dehalogenases are known as bacterial enzymes cleaving a carbon-halogen bond in halogenated compounds. Here we report the first biochemically characterized non-microbial haloalkane dehalogenase DspA from Strongylocentrotus purpuratus. The enzyme shows a preference for terminally brominated hydrocarbons and enantioselectivity towards β-brominated alkanes. Moreover, we identified other putative haloalkane dehalogenases of eukaryotic origin, representing targets for future experiments to discover dehalogenases with novel catalytic properties.
References provided by Crossref.org
Discovery of Novel Haloalkane Dehalogenase Inhibitors
