Data on the phosphorylation state of the catalytic serine of enzymes in the α-D-phosphohexomutase superfamily
Author:
Funder
National Science Foundation
Publisher
Elsevier BV
Subject
Multidisciplinary
Reference12 articles.
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3. A coevolutionary residue network at the site of a functionally important conformational change in a phosphohexomutase enzyme family;Lee;PLoS One,2012
4. Compromised catalysis and potential folding defects in in-vitro studies of missense mutants associated with hereditary phosphoglucomutase 1 deficiency;Lee;J. Biol. Chem.,2014
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1. Genetic validation of Aspergillus fumigatus phosphoglucomutase as a viable therapeutic target in invasive aspergillosis;Journal of Biological Chemistry;2022-06
2. Assessment and Impacts of Phosphorylation on Protein Flexibility of the α-d-Phosphohexomutases;Methods in Enzymology;2018
3. Phosphorylation-Dependent Effects on the Structural Flexibility of Phosphoglucosamine Mutase from Bacillus anthracis;ACS Omega;2017-11-29
4. Asp263 missense variants perturb the active site of human phosphoglucomutase 1;The FEBS Journal;2017-02-10
5. Biology, Mechanism, and Structure of Enzymes in the α- d -Phosphohexomutase Superfamily;Structural and Mechanistic Enzymology;2017
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