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Statements

Subject Item
n2:RIV%2F00216224%3A14310%2F14%3A00074206%21RIV15-MSM-14310___
rdf:type
n6:Vysledek skos:Concept
dcterms:description
Crystal structure of novel haloalkane dehalogenase DbeA revealed the presence of two chloride ions buried in the protein interior. The first halide-binding site is involved in substrate binding and is present in all structurally characterized haloalkane dehalogenases. The second halide-binding site is unique to DbeA. To elucidate the role of the second halide-binding site in enzyme functionality, a two-point mutant lacking this site was constructed and characterized. These substitutions resulted in a shift of substrate-specificity class and were accompanied by decrease of enzyme activity, stability and elimination of the substrate inhibition. The changes in enzyme catalytic activity were attributed to deceleration of the rate-limiting hydrolytic step, mediated by lower basicity of the catalytic histidine. Crystal structure of novel haloalkane dehalogenase DbeA revealed the presence of two chloride ions buried in the protein interior. The first halide-binding site is involved in substrate binding and is present in all structurally characterized haloalkane dehalogenases. The second halide-binding site is unique to DbeA. To elucidate the role of the second halide-binding site in enzyme functionality, a two-point mutant lacking this site was constructed and characterized. These substitutions resulted in a shift of substrate-specificity class and were accompanied by decrease of enzyme activity, stability and elimination of the substrate inhibition. The changes in enzyme catalytic activity were attributed to deceleration of the rate-limiting hydrolytic step, mediated by lower basicity of the catalytic histidine.
dcterms:title
Structural and Functional Analysis of a Novel Haloalkane Dehalogenase with Two Halide-Binding Sites. Structural and Functional Analysis of a Novel Haloalkane Dehalogenase with Two Halide-Binding Sites.
skos:prefLabel
Structural and Functional Analysis of a Novel Haloalkane Dehalogenase with Two Halide-Binding Sites. Structural and Functional Analysis of a Novel Haloalkane Dehalogenase with Two Halide-Binding Sites.
skos:notation
RIV/00216224:14310/14:00074206!RIV15-MSM-14310___
n3:aktivita
n17:I n17:S n17:P
n3:aktivity
I, P(GAP207/12/0775), P(LO1214), S
n3:cisloPeriodika
July
n3:dodaniDat
n14:2015
n3:domaciTvurceVysledku
n5:1030175 n5:6084559 n5:3599019 n5:2070103 n5:6975917 n5:7612656
n3:druhVysledku
n16:J
n3:duvernostUdaju
n10:S
n3:entitaPredkladatele
n4:predkladatel
n3:idSjednocenehoVysledku
47818
n3:idVysledku
RIV/00216224:14310/14:00074206
n3:jazykVysledku
n12:eng
n3:klicovaSlova
haloalkane dehalogenase DbeA from Bradyrhizobium elkanii USDA94
n3:klicoveSlovo
n13:haloalkane%20dehalogenase%20DbeA%20from%20Bradyrhizobium%20elkanii%20USDA94
n3:kodStatuVydavatele
US - Spojené státy americké
n3:kontrolniKodProRIV
[42A70CDB78D1]
n3:nazevZdroje
Acta Crystallographica D
n3:obor
n15:CE
n3:pocetDomacichTvurcuVysledku
6
n3:pocetTvurcuVysledku
13
n3:projekt
n9:LO1214 n9:GAP207%2F12%2F0775
n3:rokUplatneniVysledku
n14:2014
n3:svazekPeriodika
70
n3:tvurceVysledku
Prokop, Zbyněk Daniel, Lukáš Chaloupková, Radka Brezovský, Jan Nagata, Y. Kuta Smatanova, I. Rezacova, P. Ikeda-Ohtsubo, W. Koudeláková, Táňa Kuty, M. Prudnikova, T. Sato, Y. Damborský, Jiří
n3:wos
000338917000009
s:issn
0907-4449
s:numberOfPages
14
n18:doi
10.1107/S1399004714009018
n11:organizacniJednotka
14310