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Statements

Subject Item
n2:RIV%2F00216224%3A14310%2F13%3A00065821%21RIV14-MSM-14310___
rdf:type
n11:Vysledek skos:Concept
dcterms: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. 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.
dcterms:title
Expansion of Access Tunnels and Active-Site Cavities Influence Activity of Haloalkane Dehalogenases in Organic Cosolvents. Expansion of Access Tunnels and Active-Site Cavities Influence Activity of Haloalkane Dehalogenases in Organic Cosolvents.
skos:prefLabel
Expansion of Access Tunnels and Active-Site Cavities Influence Activity of Haloalkane Dehalogenases in Organic Cosolvents. Expansion of Access Tunnels and Active-Site Cavities Influence Activity of Haloalkane Dehalogenases in Organic Cosolvents.
skos:notation
RIV/00216224:14310/13:00065821!RIV14-MSM-14310___
n11:predkladatel
n12:orjk%3A14310
n3:aktivita
n9:P n9:I
n3:aktivity
I, P(ED0001/01/01), P(ED1.100/02/0123), P(GA203/08/0114), P(GAP503/12/0572), P(IAA401630901)
n3:cisloPeriodika
7
n3:dodaniDat
n5:2014
n3:domaciTvurceVysledku
n7:7612656 n7:1713140 n7:6084559 n7:2475960 n7:1030175 n7:3599019
n3:druhVysledku
n13:J
n3:duvernostUdaju
n16:S
n3:entitaPredkladatele
n18:predkladatel
n3:idSjednocenehoVysledku
73952
n3:idVysledku
RIV/00216224:14310/13:00065821
n3:jazykVysledku
n19:eng
n3:klicovaSlova
haloalkane dehalogenases
n3:klicoveSlovo
n17:haloalkane%20dehalogenases
n3:kodStatuVydavatele
DE - Spolková republika Německo
n3:kontrolniKodProRIV
[AC6C12132BD7]
n3:nazevZdroje
ChemBioChem
n3:obor
n15:CE
n3:pocetDomacichTvurcuVysledku
6
n3:pocetTvurcuVysledku
12
n3:projekt
n8:ED0001%2F01%2F01 n8:ED1.100%2F02%2F0123 n8:IAA401630901 n8:GAP503%2F12%2F0572 n8:GA203%2F08%2F0114
n3:rokUplatneniVysledku
n5:2013
n3:svazekPeriodika
14
n3:tvurceVysledku
Sykora, J. Khabiri, M. Chaloupková, Radka Ettrich, R. Pavelka, Antonín Prokop, Zbyněk Štěpánková, Veronika Damborský, Jiří Minofar, B. Amaro, M. Brezovský, Jan Hof, M.
n3:wos
000318280500015
s:issn
1439-4227
s:numberOfPages
8
n20:doi
10.1002/cbic.201200733
n10:organizacniJednotka
14310