Exposing catalytic versatility of GTPases: taking reaction detours in mutants of hGBP1 enzyme without additional energetic cost-Reference-Cited by-同舟云学术

Exposing catalytic versatility of GTPases: taking reaction detours in mutants of hGBP1 enzyme without additional energetic cost

Published:2019 Issue:2 Volume:21 Page:859-867
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Tripathi Ravi¹²³⁴^ORCID,Noetzel Jan¹²³⁴,Marx Dominik¹²³⁴

Affiliation:

1. Lehrstuhl für Theoretische Chemie

2. Ruhr-Universität Bochum

3. 44780 Bochum

4. Germany

Abstract

Our study reveals that the replacement of catalytically competent residues by the inert amino acid alanine, S73A and E99A, in hGBP1 opens a plethora of molecularly different reaction pathways featuring very similar energy barriers as the wild type.

Funder

Deutsche Forschungsgemeinschaft

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2019/CP/C8CP06343E

Reference60 articles.

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