Structural and functional analysis of a novel haloalkane dehalogenase with two halide-binding sites
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F14%3A43887439" target="_blank" >RIV/60076658:12310/14:43887439 - isvavai.cz</a>
Alternative codes found
RIV/60076658:12520/14:43887439
Result on the web
<a href="http://loschmidt.chemi.muni.cz/peg/wp-content/uploads/2014/07/acta14b.pdf" target="_blank" >http://loschmidt.chemi.muni.cz/peg/wp-content/uploads/2014/07/acta14b.pdf</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1107/S1399004714009018" target="_blank" >10.1107/S1399004714009018</a>
Alternative languages
Result language
angličtina
Original language name
Structural and functional analysis of a novel haloalkane dehalogenase with two halide-binding sites
Original language description
The crystal structure of the novel haloalkane dehalogenase DbeA from Bradyrhizobium elkanii USDA94 revealed the presence of two chloride ions buried in the protein interior. The first halide-binding site is involved in substrate binding and is present inall structurally characterized haloalkane dehalogenases. The second halide-binding site is unique to DbeA. To elucidate the role of the second halide-binding site in enzyme functionality, a two-point mutant lacking this site was constructed and characterized. These substitutions resulted in a shift in the substrate-specificity class and were accompanied by a decrease in enzyme activity, stability and the elimination of substrate inhibition. The changes in enzyme catalytic activity were attributed to deceleration of the rate-limiting hydrolytic step mediated by the lower basicity of the catalytic histidine.
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
<a href="/en/project/GAP207%2F12%2F0775" target="_blank" >GAP207/12/0775: Structure-functional Relationships of Haloalkane Dehalogenases</a><br>
Continuities
S - Specificky vyzkum na vysokych skolach
Others
Publication year
2014
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Acta Crystallographica Section D - Biological Crystallography
ISSN
1399-0047
e-ISSN
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Volume of the periodical
70
Issue of the periodical within the volume
JUL 2014
Country of publishing house
US - UNITED STATES
Number of pages
14
Pages from-to
1884-1897
UT code for WoS article
000338917000009
EID of the result in the Scopus database
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