Comparative binding energy (COMBINE) analysis of the substrate specificity of haloalkane dehalogenase from Xanthobacter autotrophicus GJ10

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F01%3A00004531" target="_blank" >RIV/00216224:14310/01:00004531 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Comparative binding energy (COMBINE) analysis of the substrate specificity of haloalkane dehalogenase from Xanthobacter autotrophicus GJ10

Popis výsledku v původním jazyce

Comparative binding energy (COMBINE) analysis was conducted for eighteen substrates of the haloalkane dehalogenase from Xanthobacter autotrophicus GJ10: 1-chlorobutane; 1-chlorohexane; dichloromethane; 1,2-dichloroethane; 1,2-dichloropropane; 2-chloroethanol; epichlorohydrine; 2-chloroacetonitrile, 2-chloroacetamide and their brominated analogs. The purpose of the COMBINE analysis was to identify the amino acid residues determining the substrate specificity of the haloalkane dehalogenase. This knowledgeis essential for the tailoring of this enzyme for biotechnological applications. Complexes of the enzyme with these substrates were modeled and then refined by molecular mechanics energy minimization. The intermolecular enzyme-substrate energy was decomposed into residue-wise van der Waals and electrostatic contributions and complemented by surface area dependent and electrostatic desolvation terms. Partial least-squares projection to latent structures analysis was then used to establis

Název v anglickém jazyce

Comparative binding energy (COMBINE) analysis of the substrate specificity of haloalkane dehalogenase from Xanthobacter autotrophicus GJ10

Popis výsledku anglicky

Comparative binding energy (COMBINE) analysis was conducted for eighteen substrates of the haloalkane dehalogenase from Xanthobacter autotrophicus GJ10: 1-chlorobutane; 1-chlorohexane; dichloromethane; 1,2-dichloroethane; 1,2-dichloropropane; 2-chloroethanol; epichlorohydrine; 2-chloroacetonitrile, 2-chloroacetamide and their brominated analogs. The purpose of the COMBINE analysis was to identify the amino acid residues determining the substrate specificity of the haloalkane dehalogenase. This knowledgeis essential for the tailoring of this enzyme for biotechnological applications. Complexes of the enzyme with these substrates were modeled and then refined by molecular mechanics energy minimization. The intermolecular enzyme-substrate energy was decomposed into residue-wise van der Waals and electrostatic contributions and complemented by surface area dependent and electrostatic desolvation terms. Partial least-squares projection to latent structures analysis was then used to establis

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/LN00A016" target="_blank" >LN00A016: BIOMOLEKULÁRNÍ CENTRUM</a><br>

Návaznosti

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

Rok uplatnění

2001

Kód důvěrnosti údajů

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

Název periodika

Biochemistry

ISSN

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e-ISSN

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Svazek periodika

40

Číslo periodika v rámci svazku

30

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

13

Strana od-do

8905

Kód UT WoS článku

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EID výsledku v databázi Scopus

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