Structural and functional analysis of a novel haloalkane dehalogenase with two halide-binding sites
Identifikátory výsledku
Kód výsledku v 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>
Nalezeny alternativní kódy
RIV/60076658:12520/14:43887439
Výsledek na webu
<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>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Structural and functional analysis of a novel haloalkane dehalogenase with two halide-binding sites
Popis výsledku v původním jazyce
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.
Název v anglickém jazyce
Structural and functional analysis of a novel haloalkane dehalogenase with two halide-binding sites
Popis výsledku anglicky
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.
Klasifikace
Druh
J<sub>x</sub> - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)
CEP obor
CE - Biochemie
OECD FORD obor
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Návaznosti výsledku
Projekt
<a href="/cs/project/GAP207%2F12%2F0775" target="_blank" >GAP207/12/0775: Strukturně-funkční vztahy haloalkan dehalogenas</a><br>
Návaznosti
S - Specificky vyzkum na vysokych skolach
Ostatní
Rok uplatnění
2014
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Acta Crystallographica Section D - Biological Crystallography
ISSN
1399-0047
e-ISSN
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Svazek periodika
70
Číslo periodika v rámci svazku
JUL 2014
Stát vydavatele periodika
US - Spojené státy americké
Počet stran výsledku
14
Strana od-do
1884-1897
Kód UT WoS článku
000338917000009
EID výsledku v databázi Scopus
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