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Statements

Subject Item
n2:RIV%2F00216224%3A14310%2F02%3A00006914%21RIV08-MSM-14310___
rdf:type
skos:Concept n19:Vysledek
dcterms:description
Haloalkane dehalogenases catalyze cleavage of the carbon-halogen bond in halogenated aliphatic compounds resulting in the formation of an alcohol, a halide and a proton as the reaction products. Three structural features of haloalkane dehalogenases are essential for their catalytic performance: (i) a catalytic triad, (ii) an oxyanion hole and (iii) the halide-stabilizing residues. Halide-stabilizing residues are not structurally conserved among different haloalkane dehalogenases. The level of stabilization of the transition state structure of SN2 reaction and halide ion provided by each of the active site residues in the enzymes DhlA, LinB and DhaA was quantified by quantum mechanic calculations. The residues that significantly stabilize the halide ion were assigned as the primary (essential) or the secondary (less important) halide-stabilizing residues. Site-directed mutagenesis was conducted with LinB enzyme to confirm location of its primary halide-stabilizing residues. Asn38Asp, Asn38Glu, Asn38Phe Haloalkane dehalogenases catalyze cleavage of the carbon-halogen bond in halogenated aliphatic compounds resulting in the formation of an alcohol, a halide and a proton as the reaction products. Three structural features of haloalkane dehalogenases are essential for their catalytic performance: (i) a catalytic triad, (ii) an oxyanion hole and (iii) the halide-stabilizing residues. Halide-stabilizing residues are not structurally conserved among different haloalkane dehalogenases. The level of stabilization of the transition state structure of SN2 reaction and halide ion provided by each of the active site residues in the enzymes DhlA, LinB and DhaA was quantified by quantum mechanic calculations. The residues that significantly stabilize the halide ion were assigned as the primary (essential) or the secondary (less important) halide-stabilizing residues. Site-directed mutagenesis was conducted with LinB enzyme to confirm location of its primary halide-stabilizing residues. Asn38Asp, Asn38Glu, Asn38Phe Haloalkane dehalogenases catalyze cleavage of the carbon-halogen bond in halogenated aliphatic compounds resulting in the formation of an alcohol, a halide and a proton as the reaction products. Three structural features of haloalkane dehalogenases are essential for their catalytic performance: (i) a catalytic triad, (ii) an oxyanion hole and (iii) the halide-stabilizing residues. Halide-stabilizing residues are not structurally conserved among different haloalkane dehalogenases. The level of stabilization of the transition state structure of SN2 reaction and halide ion provided by each of the active site residues in the enzymes DhlA, LinB and DhaA was quantified by quantum mechanic calculations. The residues that significantly stabilize the halide ion were assigned as the primary (essential) or the secondary (less important) halide-stabilizing residues. Site-directed mutagenesis was conducted with LinB enzyme to confirm location of its primary halide-stabilizing residues. Asn38Asp, Asn38Glu, Asn38Phe
dcterms:title
Halide-stabilizing residues of haloalkane dehalogenases studied by quantum mechanic calculations and site-directed mutagenesis Halide-stabilizing residues of haloalkane dehalogenases studied by quantum mechanic calculations and site-directed mutagenesis Halide-stabilizing residues of haloalkane dehalogenases studied by quantum mechanic calculations and site-directed mutagenesis
skos:prefLabel
Halide-stabilizing residues of haloalkane dehalogenases studied by quantum mechanic calculations and site-directed mutagenesis Halide-stabilizing residues of haloalkane dehalogenases studied by quantum mechanic calculations and site-directed mutagenesis Halide-stabilizing residues of haloalkane dehalogenases studied by quantum mechanic calculations and site-directed mutagenesis
skos:notation
RIV/00216224:14310/02:00006914!RIV08-MSM-14310___
n3:strany
14272
n3:aktivita
n5:Z n5:P
n3:aktivity
P(ME 276), Z(MSM 143100005)
n3:cisloPeriodika
48
n3:dodaniDat
n7:2008
n3:domaciTvurceVysledku
n12:1030175 n12:3599019 n12:9561900 n12:4347374 n12:7970129 n12:3993779
n3:druhVysledku
n10:J
n3:duvernostUdaju
n8:S
n3:entitaPredkladatele
n4:predkladatel
n3:idSjednocenehoVysledku
647382
n3:idVysledku
RIV/00216224:14310/02:00006914
n3:jazykVysledku
n18:eng
n3:klicovaSlova
QUANTUM MECHANICS; HALIDE; MUTANT; PROTEIN ENGINEERING; STABILISATION
n3:klicoveSlovo
n11:MUTANT n11:QUANTUM%20MECHANICS n11:PROTEIN%20ENGINEERING n11:STABILISATION n11:HALIDE
n3:kodStatuVydavatele
US - Spojené státy americké
n3:kontrolniKodProRIV
[FC9D83753F57]
n3:nazevZdroje
Biochemistry
n3:obor
n16:CE
n3:pocetDomacichTvurcuVysledku
6
n3:pocetTvurcuVysledku
8
n3:projekt
n15:ME%20276
n3:rokUplatneniVysledku
n7:2002
n3:svazekPeriodika
41
n3:tvurceVysledku
Koča, Jaroslav Nagata, Yuji Prokop, Martin Monincová, Marta Prokop, Zbyněk Damborský, Jiří Boháč, Michal Tsuda, Masataka
n3:zamer
n13:MSM%20143100005
s:issn
0006-2960
s:numberOfPages
9
n14:organizacniJednotka
14310