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Biochemical characteristics of the novel haloalkane dehalogenase DatA, isolated from the plant pathogen Agrobacterium tumefaciens C58
K. Hasan, A. Fortova, T. Koudelakova, R. Chaloupkova, M. Ishitsuka, Y. Nagata, J. Damborsky, Z. Prokop
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
21193677
DOI
10.1128/aem.02109-10
Knihovny.cz E-resources
- MeSH
- Agrobacterium tumefaciens enzymology genetics metabolism MeSH
- Alkanes metabolism MeSH
- DNA, Bacterial chemistry genetics MeSH
- Esters metabolism MeSH
- Hydrolases genetics isolation & purification metabolism MeSH
- Molecular Sequence Data MeSH
- Protein Multimerization MeSH
- Plants microbiology MeSH
- Sequence Analysis, DNA MeSH
- Stereoisomerism MeSH
- Substrate Specificity MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
We report the biochemical characterization of a novel haloalkane dehalogenase, DatA, isolated from the plant pathogen Agrobacterium tumefaciens C58. DatA possesses a peculiar pair of halide-stabilizing residues, Asn-Tyr, which have not been reported to play this role in other known haloalkane dehalogenases. DatA has a number of other unique characteristics, including substrate-dependent and cooperative kinetics, a dimeric structure, and excellent enantioselectivity toward racemic mixtures of chiral brominated alkanes and esters.
References provided by Crossref.org
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