Cation-Specific Effects on Enzymatic Catalysis Driven by Interactions at the Tunnel Mouth

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F13%3A00394029" target="_blank" >RIV/61388963:_____/13:00394029 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216224:14310/13:00066616 RIV/00159816:_____/13:00060623

Výsledek na webu

<a href="http://dx.doi.org/10.1021/jp401506v" target="_blank" >http://dx.doi.org/10.1021/jp401506v</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1021/jp401506v" target="_blank" >10.1021/jp401506v</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Cation-Specific Effects on Enzymatic Catalysis Driven by Interactions at the Tunnel Mouth

Popis výsledku v původním jazyce

Cationic specificity which follows the Hofmeister series has, been established for the catalytic efficiency of haloalkane dehalogenase LinB by a combination of molecular dynamics simulations and enzyme kinetic experiments. Simulations provided a detailedmolecular picture of cation interactions with negatively charged residues on the protein surface, particularly at the tunnel mouth leading to the enzyme active site. On the basis of the binding affinities, cations were ordered as Na+ > K+ > Rb+ > Cs+. In agreement with this result, a steady-state kinetic analysis disclosed that the smaller alkali cations influence formation and productivity of enzyme-substrate complexes more efficiently than the larger ones. A subsequent systematic investigation of twoLinB mutants with engineered charge in the cation-binding site revealed that the observed cation affinities are enhanced by increasing the number of negatively charged residues at the tunnel mouth, and vice versa, reduced by decreasing t

Název v anglickém jazyce

Cation-Specific Effects on Enzymatic Catalysis Driven by Interactions at the Tunnel Mouth

Popis výsledku anglicky

Cationic specificity which follows the Hofmeister series has, been established for the catalytic efficiency of haloalkane dehalogenase LinB by a combination of molecular dynamics simulations and enzyme kinetic experiments. Simulations provided a detailedmolecular picture of cation interactions with negatively charged residues on the protein surface, particularly at the tunnel mouth leading to the enzyme active site. On the basis of the binding affinities, cations were ordered as Na+ > K+ > Rb+ > Cs+. In agreement with this result, a steady-state kinetic analysis disclosed that the smaller alkali cations influence formation and productivity of enzyme-substrate complexes more efficiently than the larger ones. A subsequent systematic investigation of twoLinB mutants with engineered charge in the cation-binding site revealed that the observed cation affinities are enhanced by increasing the number of negatively charged residues at the tunnel mouth, and vice versa, reduced by decreasing t

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CF - Fyzikální chemie a teoretická chemie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2013

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Journal of Physical Chemistry B

ISSN

1520-6106

e-ISSN

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Svazek periodika

117

Číslo periodika v rámci svazku

21

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

9

Strana od-do

6394-6402

Kód UT WoS článku

000319896800006

EID výsledku v databázi Scopus

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