Brave new surfactant world revisited by thermoalkalophilic lipases: computational insights into the role of SDS as a substrate analog-Reference-Cited by-同舟云学术

Brave new surfactant world revisited by thermoalkalophilic lipases: computational insights into the role of SDS as a substrate analog

Published:2023 Issue:3 Volume:25 Page:2234-2247
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Shehata Mohamed¹,Ünlü Aişe²^ORCID,Iglesias-Fernández Javier³,Osuna Sílvia⁴⁵,Sezerman O Ugur¹,Timucin Emel¹^ORCID

Affiliation:

1. Department of Biostatistics and Medical Informatics, School of Medicine, Acibadem University, Istanbul 34752, Turkey

2. Department of Chemistry, Gebze Technical University, Kocaeli, Turkey

3. Nostrum Biodiscovery, S.L., E-08029 Barcelona, Spain

4. CompBioLab Group, Institut de Química Computacional i Catàlisi (IQCC) and Department de Química, Universitat de Girona, c/Maria Aurèlia Capmany 69, 17003 Girona, Spain

5. ICREA, Pg. Lluís Companys 23, 08010 Barcelona, Spain

Abstract

SDS binds to the catalytic cleft of a thermostable lipase and partially opens its closed lid.

Funder

Ministerio de Economía y Competitividad

H2020 European Research Council

Human Frontier Science Program

Agència de Gestió d'Ajuts Universitaris i de Recerca

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2023/CP/D2CP05093E

Reference87 articles.

1. News from the interface: the molecular structures of triacyglyceride lipases

2. Enhancing catalytic promiscuity for biocatalysis

3. Lipases: Useful biocatalysts for the preparation of pharmaceuticals

4. Molecular Modeling Investigation of the Interaction between Humicola insolens Cutinase and SDS Surfactant Suggests a Mechanism for Enzyme Inactivation

5. Interaction of a digestive protease, Candida rugosa lipase, with three surfactants investigated by spectroscopy, molecular docking and enzyme activity assay

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