Universality of critical active site glutamate as an acid–base catalyst in serine hydroxymethyltransferase function-Reference-Cited by-同舟云学术

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Universality of critical active site glutamate as an acid–base catalyst in serine hydroxymethyltransferase function

Published:2024 Issue:32 Volume:15 Page:12827-12844
ISSN:2041-6520
Container-title:Chemical Science
language:en
Short-container-title:Chem. Sci.

Author:

Drago Victoria N.¹^ORCID,Phillips Robert S.²³^ORCID,Kovalevsky Andrey¹^ORCID

Affiliation:

1. Neutron Scattering Division, Oak Ridge National Laboratory, Oak Ridge, TN, 37831, USA

2. Department of Chemistry, University of Georgia, Athens, GA, 30602, USA

3. Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA, 30602, USA

Abstract

Neutron crystallography revealed protonation states in TthSHMT-FA complex. Glu53 is protonated but other residues maintain protonation states upon FA binding. Structural analyses support key roles of Glu53 and gating loop dynamics in SHMT function.

Funder

National Institute of General Medical Sciences

Biological and Environmental Research

Office of Science

U.S. Department of Energy

Argonne National Laboratory

Publisher

Royal Society of Chemistry (RSC)

Link

http://pubs.rsc.org/en/content/articlepdf/2024/SC/D4SC03187C

Reference85 articles.

1. A genomic overview of pyridoxal‐phosphate‐dependent enzymes

2. Cytoplasmic Serine Hydroxymethyltransferase Mediates Competition between Folate-dependent Deoxyribonucleotide andS-Adenosylmethionine Biosyntheses

3. Serine hydroxymethyltransferase 2: a novel target for human cancer therapy

4. Serine hydroxymethyltransferase: mechanism of the racemization and transamination of D- and L-alanine

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