Modulation of global stability, ligand binding and catalytic properties of trypsin by anions

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F22%3A00565456" target="_blank" >RIV/61388971:_____/22:00565456 - isvavai.cz</a>

Alternative codes found

RIV/60076658:12310/22:43905988

Result on the web

<a href="https://www.sciencedirect.com/science/article/pii/S0301462222000989?via%3Dihub" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0301462222000989?via%3Dihub</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.bpc.2022.106856" target="_blank" >10.1016/j.bpc.2022.106856</a>

Result language

angličtina

Original language name

Modulation of global stability, ligand binding and catalytic properties of trypsin by anions

Original language description

Specific salts effect is well-known on stability and solubility of proteins, however, relatively limited knowledge is known regarding the effect on catalytic properties of enzymes. Here, we examined the effect of four sodium anions on thermal stability and catalytic properties of trypsin and binding of the fluorescent probe, p-aminobenzamidine (PAB), to the enzyme. We show that the specific anions effect on trypsin properties agrees with the localization of the anions in the Hofmeister series. Thermal stability of trypsin, Tm, the affinity of the fluorescent probe to the binding site, Kd, and the rate constant, kcat, of trypsin-catalyzed hydrolysis of the substrate N-benzoyl-L-arginine ethyl ester (BAEE) increase with increasing kosmotropic character of anions in the order: perchlorate<bromide<chloride<sulfate, while the value of Michaelis constant, KM, decreases. Correlations between the values of Tm, Kd for PAB, kcat, and KM for BAEE in the presence of 1 M studied salts suggest interrelation among these parameters of the enzyme. Global stabilization as well as increased rigidity of trypsin is accompanied by strengthening of interaction with fluorescent probe PAB and in accordance with decreasing values of KM for the substrate BAEE. Strong correlations between parameters characterizing the trypsin properties with the charge densities of anions clearly indicate direct electrostatic interaction as a basis of the specific anion effect on the conformational and functional properties of the enzyme.

Czech name

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Czech description

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Type

J_SC - Article in a specialist periodical, which is included in the SCOPUS database

CEP classification

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OECD FORD branch

10610 - Biophysics

Project

<a href="/en/project/GA21-15936S" target="_blank" >GA21-15936S: Effects of Macromolecular Crowding on Enzyme Structure and Kinetics</a><br>

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2022

Confidentiality

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

Name of the periodical

Biophysical Chemistry

ISSN

0301-4622

e-ISSN

1873-4200

Volume of the periodical

288

Issue of the periodical within the volume

September 2022

Country of publishing house

NL - THE KINGDOM OF THE NETHERLANDS

Number of pages

10

Pages from-to

106856

UT code for WoS article

—

EID of the result in the Scopus database

2-s2.0-85134602630