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Statements

Subject Item
n2:RIV%2F00216224%3A14310%2F14%3A00074209%21RIV15-MSM-14310___
rdf:type
skos:Concept n15:Vysledek
dcterms:description
We emphasize the importance of dynamics and hydration for enzymatic catalysis and protein design by transplanting the active site from a haloalkane dehalogenase with high enantioselectivity to nonselective dehalogenase. Protein crystallography confirms that the active site geometry of the redesigned dehalogenase matches that of the target, but its enantioselectivity remains low. Time-dependent fluorescence shifts and computer simulations revealed that dynamics and hydration at the tunnel mouth differ substantially between the redesigned and target dehalogenase. We emphasize the importance of dynamics and hydration for enzymatic catalysis and protein design by transplanting the active site from a haloalkane dehalogenase with high enantioselectivity to nonselective dehalogenase. Protein crystallography confirms that the active site geometry of the redesigned dehalogenase matches that of the target, but its enantioselectivity remains low. Time-dependent fluorescence shifts and computer simulations revealed that dynamics and hydration at the tunnel mouth differ substantially between the redesigned and target dehalogenase.
dcterms:title
Dynamics and Hydration Explain Failed Functional Transformation in Dehalogenase Design. Dynamics and Hydration Explain Failed Functional Transformation in Dehalogenase Design.
skos:prefLabel
Dynamics and Hydration Explain Failed Functional Transformation in Dehalogenase Design. Dynamics and Hydration Explain Failed Functional Transformation in Dehalogenase Design.
skos:notation
RIV/00216224:14310/14:00074209!RIV15-MSM-14310___
n3:aktivita
n6:P n6:I
n3:aktivity
I, P(ED1.100/02/0123), P(EE2.3.30.0037), P(GAP503/12/0572), P(GBP208/12/G016), P(LO1214)
n3:cisloPeriodika
6
n3:dodaniDat
n12:2015
n3:domaciTvurceVysledku
n11:6084559 n11:3599019 n11:7612656 n11:9123377 n11:1713140 n11:1030175 n11:2070103
n3:druhVysledku
n7:J
n3:duvernostUdaju
n16:S
n3:entitaPredkladatele
n13:predkladatel
n3:idSjednocenehoVysledku
12724
n3:idVysledku
RIV/00216224:14310/14:00074209
n3:jazykVysledku
n8:eng
n3:klicovaSlova
haloalkane dehalogenase
n3:klicoveSlovo
n17:haloalkane%20dehalogenase
n3:kodStatuVydavatele
US - Spojené státy americké
n3:kontrolniKodProRIV
[DF36122EBB67]
n3:nazevZdroje
Nature Chemical Biology
n3:obor
n18:CE
n3:pocetDomacichTvurcuVysledku
7
n3:pocetTvurcuVysledku
12
n3:projekt
n9:EE2.3.30.0037 n9:ED1.100%2F02%2F0123 n9:LO1214 n9:GAP503%2F12%2F0572 n9:GBP208%2F12%2FG016
n3:rokUplatneniVysledku
n12:2014
n3:svazekPeriodika
10
n3:tvurceVysledku
Fořtová, Andrea Sykora, J. Prokop, Zbyněk Koudeláková, Táňa Hof, M. Chaloupková, Radka Kuta Smatanova, I. Damborský, Jiří Chernovets, T. Lahoda, M. Brezovský, Jan Štěpánková, Veronika
n3:wos
000336238200008
s:issn
1552-4450
s:numberOfPages
3
n14:organizacniJednotka
14310