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Biochemical characterization of a novel haloalkane dehalogenase from a cold-adapted bacterium
I. Drienovska, E. Chovancova, T. Koudelakova, J. Damborsky, R. Chaloupkova,
Language English Country United States
Document type Journal Article, Research Support, Non-U.S. Gov't
NLK
Free Medical Journals
from 1976 to 6 months ago
PubMed Central
from 1976 to 1 year ago
Europe PubMed Central
from 1976 to 6 months ago
Open Access Digital Library
from 1953-01-01
PubMed
22582053
DOI
10.1128/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
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.
References provided by Crossref.org
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