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Statements

Subject Item
n2:RIV%2F00216208%3A11310%2F13%3A10134075%21RIV14-GA0-11310___
rdf:type
skos:Concept n12:Vysledek
rdfs:seeAlso
http://dx.doi.org/10.1039/c2fd20094e
dcterms:description
Human immunodeficiency virus 1 protease (HIV-1 PR), an important therapeutic target for the treatment of AIDS, is one of the most well-studied enzymes. However, there is still much to learn about the regulation of the activity and inhibition of this key viral enzyme. Specifically, the mechanism of activation of HIV-1 PR from the viral polyprotein upon HIV maturation is still not understood. It has been suggested that external factors like pH or salt concentration might contribute to regulation of this crucial step in the viral life cycle. Recently, we analyzed the activity of HIV-1 PR in aqueous solutions of sodium and potassium chloride by experimental determination of enzyme kinetics and molecular dynamics simulations. We showed that the effect of salt concentration is cation-specific [Heyda et al., Phys. Chem. Chem. Phys., 2009 (11), 7599]. In this study, we extended this analysis for other alkali cations and found that the dependence of the initial velocity of peptide substrate hydrolysis on the nature of the cation follows the Hofmeister series, with the exception of caesium. Significantly higher catalytic efficiencies both in terms of substrate binding (K-M) and turnover number (k(cat)) are observed in the presence of K+ compared to Na+ or Li+ at corresponding salt concentrations. Molecular dynamics simulations suggest that both lithium and sodium are attracted more strongly than potassium and caesium to the protein surface, mostly due to stronger interactions with carboxylate side chain groups of aspartates and glutamates. Furthermore, we observed a surprising decrease in the K-M value for a specific substrate at very low salt concentration. The molecular mechanism of this phenomenon will be further analyzed. Human immunodeficiency virus 1 protease (HIV-1 PR), an important therapeutic target for the treatment of AIDS, is one of the most well-studied enzymes. However, there is still much to learn about the regulation of the activity and inhibition of this key viral enzyme. Specifically, the mechanism of activation of HIV-1 PR from the viral polyprotein upon HIV maturation is still not understood. It has been suggested that external factors like pH or salt concentration might contribute to regulation of this crucial step in the viral life cycle. Recently, we analyzed the activity of HIV-1 PR in aqueous solutions of sodium and potassium chloride by experimental determination of enzyme kinetics and molecular dynamics simulations. We showed that the effect of salt concentration is cation-specific [Heyda et al., Phys. Chem. Chem. Phys., 2009 (11), 7599]. In this study, we extended this analysis for other alkali cations and found that the dependence of the initial velocity of peptide substrate hydrolysis on the nature of the cation follows the Hofmeister series, with the exception of caesium. Significantly higher catalytic efficiencies both in terms of substrate binding (K-M) and turnover number (k(cat)) are observed in the presence of K+ compared to Na+ or Li+ at corresponding salt concentrations. Molecular dynamics simulations suggest that both lithium and sodium are attracted more strongly than potassium and caesium to the protein surface, mostly due to stronger interactions with carboxylate side chain groups of aspartates and glutamates. Furthermore, we observed a surprising decrease in the K-M value for a specific substrate at very low salt concentration. The molecular mechanism of this phenomenon will be further analyzed.
dcterms:title
Ion specific effects of alkali cations on the catalytic activity of HIV-1 protease Ion specific effects of alkali cations on the catalytic activity of HIV-1 protease
skos:prefLabel
Ion specific effects of alkali cations on the catalytic activity of HIV-1 protease Ion specific effects of alkali cations on the catalytic activity of HIV-1 protease
skos:notation
RIV/00216208:11310/13:10134075!RIV14-GA0-11310___
n12:predkladatel
n13:orjk%3A11310
n3:aktivita
n10:I n10:P
n3:aktivity
I, P(GAP207/11/1798), P(GBP208/12/G016)
n3:cisloPeriodika
leden 2013
n3:dodaniDat
n16:2014
n3:domaciTvurceVysledku
n11:7120532
n3:druhVysledku
n9:J
n3:duvernostUdaju
n4:S
n3:entitaPredkladatele
n19:predkladatel
n3:idSjednocenehoVysledku
81195
n3:idVysledku
RIV/00216208:11310/13:10134075
n3:jazykVysledku
n18:eng
n3:klicovaSlova
halides; potassium; salt; state; binding; inhibitors; force-field; molecular-dynamics; retroviral proteases; hofmeister series
n3:klicoveSlovo
n5:state n5:inhibitors n5:molecular-dynamics n5:retroviral%20proteases n5:force-field n5:potassium n5:binding n5:hofmeister%20series n5:halides n5:salt
n3:kodStatuVydavatele
GB - Spojené království Velké Británie a Severního Irska
n3:kontrolniKodProRIV
[4ED490CED87B]
n3:nazevZdroje
Faraday Discussions
n3:obor
n21:CE
n3:pocetDomacichTvurcuVysledku
1
n3:pocetTvurcuVysledku
3
n3:projekt
n17:GBP208%2F12%2FG016 n17:GAP207%2F11%2F1798
n3:rokUplatneniVysledku
n16:2013
n3:svazekPeriodika
160
n3:tvurceVysledku
Heyda, Jan Pokorná, Jana Konvalinka, Jan
n3:wos
000313815400023
s:issn
1359-6640
s:numberOfPages
12
n7:doi
10.1039/c2fd20094e
n6:organizacniJednotka
11310