Structural and Functional Analysis of a Novel Haloalkane Dehalogenase with Two Halide-Binding Sites.

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F14%3A00074206" target="_blank" >RIV/00216224:14310/14:00074206 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/67179843:_____/14:00430522 RIV/61388963:_____/14:00430522

Výsledek na webu

<a href="http://dx.doi.org/10.1107/S1399004714009018" target="_blank" >http://dx.doi.org/10.1107/S1399004714009018</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1107/S1399004714009018" target="_blank" >10.1107/S1399004714009018</a>

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

Crystal structure of novel haloalkane dehalogenase DbeA 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 in all structurally characterized haloalkanedehalogenases. 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 of substrate-specificity class and were accompanied by decrease of enzyme activity, stability and elimination of the substrate inhibition. The changes in enzyme catalytic activity were attributed to deceleration of the rate-limiting hydrolytic step,mediated by 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

Crystal structure of novel haloalkane dehalogenase DbeA 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 in all structurally characterized haloalkanedehalogenases. 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 of substrate-specificity class and were accompanied by decrease of enzyme activity, stability and elimination of the substrate inhibition. The changes in enzyme catalytic activity were attributed to deceleration of the rate-limiting hydrolytic step,mediated by lower basicity of the catalytic histidine.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

—

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2014

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Acta Crystallographica D

ISSN

0907-4449

e-ISSN

—

Svazek periodika

70

Číslo periodika v rámci svazku

July

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

—