How inverting β-1,4-galactosyltransferase-1 can quench a high charge of the by-product UDP3−in catalysis: a QM/MM study of enzymatic reaction with native and UDP-5′ thio galactose substrates-Reference-Cited by-同舟云学术

How inverting β-1,4-galactosyltransferase-1 can quench a high charge of the by-product UDP3−in catalysis: a QM/MM study of enzymatic reaction with native and UDP-5′ thio galactose substrates

Published:2020 Issue:38 Volume:18 Page:7585-7596
ISSN:1477-0520
Container-title:Organic & Biomolecular Chemistry
language:en
Short-container-title:Org. Biomol. Chem.

Author:

Kóňa J.¹²³⁴⁵^ORCID

Affiliation:

1. Institute of Chemistry

2. Center for Glycomics

3. Slovak Academy of Sciences

4. 84538 Bratislava

5. Slovak Republic

Abstract

The function of Asp252 in the catalysis of β-1,4-galactosyltransferase-1 may be the stabilization of a high charge of the by-product UDP³⁻by a substrate-assisted proton transfer reaction.

Funder

Agentúra na Podporu Výskumu a Vývoja

Vedecká Grantová Agentúra MŠVVaŠ SR a SAV

Slovenská Akadémia Vied

Publisher

Royal Society of Chemistry (RSC)

Subject

Organic Chemistry,Physical and Theoretical Chemistry,Biochemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2020/OB/D0OB01490G

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