Biochemical characterization of a novel haloalkane dehalogenase from a cold-adapted bacterium
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
22582053
PubMed Central
PMC3416366
DOI
10.1128/aem.00485-12
PII: AEM.00485-12
Knihovny.cz E-resources
- MeSH
- Bacterial Proteins chemistry genetics metabolism MeSH
- Adaptation, Physiological * MeSH
- Hydrolases chemistry genetics metabolism MeSH
- Kinetics MeSH
- Hydrogen-Ion Concentration MeSH
- Cold Temperature * MeSH
- Psychrobacter enzymology genetics growth & development physiology MeSH
- Substrate Specificity MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Bacterial Proteins MeSH
- haloalkane dehalogenase MeSH Browser
- Hydrolases MeSH
A haloalkane dehalogenase, DpcA, from Psychrobacter cryohalolentis K5, representing a novel psychrophilic member of the haloalkane dehalogenase family, was identified and biochemically characterized. DpcA exhibited a unique temperature profile with exceptionally high activities at low temperatures. The psychrophilic properties of DpcA make this enzyme promising for various environmental applications.
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