Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adaptation, Physiological*
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Bacterial Proteins / chemistry
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism
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Cold Temperature*
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Hydrogen-Ion Concentration
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Hydrolases / chemistry
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Hydrolases / genetics
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Hydrolases / metabolism*
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Kinetics
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Psychrobacter / enzymology*
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Psychrobacter / genetics
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Psychrobacter / growth & development
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Psychrobacter / physiology
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Substrate Specificity
Substances
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Bacterial Proteins
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Hydrolases
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haloalkane dehalogenase