Expansion of Access Tunnels and Active-Site Cavities Influence Activity of Haloalkane Dehalogenases in Organic Cosolvents.

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F13%3A00065821" target="_blank" >RIV/00216224:14310/13:00065821 - isvavai.cz</a>

Alternative codes found

RIV/67179843:_____/13:00392431 RIV/61388955:_____/13:00392431 RIV/60076658:12310/13:43885643 RIV/00159816:_____/13:00060562

Result on the web

<a href="http://dx.doi.org/10.1002/cbic.201200733" target="_blank" >http://dx.doi.org/10.1002/cbic.201200733</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1002/cbic.201200733" target="_blank" >10.1002/cbic.201200733</a>

Result language

angličtina

Original language name

Expansion of Access Tunnels and Active-Site Cavities Influence Activity of Haloalkane Dehalogenases in Organic Cosolvents.

Original language description

The use of enzymes for biocatalysis can be significantly enhanced by using organic cosolvents in the reaction mixtures. Selection of the cosolvent type and concentration range for an enzymatic reaction is challenging and requires extensive empirical testing. An understanding of protein-solvent interaction could provide a theoretical framework for rationalising the selection process. Here, the behaviour of three model enzymes (haloalkane dehalogenases) was investigated in the presence of three representative organic cosolvents (acetone, formamide, and isopropanol). Steady-state kinetics assays, molecular dynamics simulations, and time-resolved fluorescence spectroscopy were used to elucidate the molecular mechanisms of enzyme-solvent interactions. Cosolvent molecules entered the enzymes? access tunnels and active sites, enlarged their volumes with no change in overall protein structure, but surprisingly did not act as competitive inhibitors.

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

CE - Biochemistry

OECD FORD branch

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Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

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

Publication year

2013

Confidentiality

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

Name of the periodical

ChemBioChem

ISSN

1439-4227

e-ISSN

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Volume of the periodical

14

Issue of the periodical within the volume

7

Country of publishing house

DE - GERMANY

Number of pages

8

Pages from-to

890-897

UT code for WoS article

000318280500015

EID of the result in the Scopus database

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