ArticleThe FEBS journal2017
Asp263 missense variants perturb the active site of human phosphoglucomutase 1.
Article in The FEBS journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 14 citations in OpenAlex.
- Article
- Effects of the T337M and G391V disease-related variants on human phosphoglucomutase 1: structural disruptions large and small.Acta crystallographica. Section F, Structural biology communications · 2022Article
- Structural basis for substrate and product recognition in human phosphoglucomutase-1 (PGM1) isoform 2, a member of the α-D-phosphohexomutase superfamily.Scientific reports · 2020Article
- HeterozygousFrontiers in genetics · 2020Article
- Structural and dynamical description of the enzymatic reaction of a phosphohexomutase.Structural dynamics (Melville, N.Y.) · 2019Article
- A Hotspot for Disease-Associated Variants of Human PGM1 Is Associated with Impaired Ligand Binding and Loop Dynamics.Structure (London, England : 1993) · 2018Article
- Mechanistic Insights on Human Phosphoglucomutase Revealed by Transition Path Sampling and Molecular Dynamics Calculations.Chemistry (Weinheim an der Bergstrasse, Germany) · 2018Article
- Sequence-structure relationships, expression profiles, and disease-associated mutations in the paralogs of phosphoglucomutase 1.PloS one · 2017Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The enzyme phosphoglucomutase 1 (PGM1) plays a central role in glucose homeostasis. Clinical studies have identified mutations in human PGM1 as the cause of PGM1 deficiency, an inherited metabolic disease. One residue, Asp263, has two known variants associated with disease: D263G and D263Y. Biochemical studies have shown that these mutants are soluble and well folded, but have significant catalytic impairment. To better understand this catalytic defect, we determined crystal structures of these two missense variants, both of which reveal a similar and indirect structural change due to the loss of a conserved salt bridge between Asp263 and Arg293. The arginine reorients into the active site, making interactions with residues responsible for substrate binding. Biochemical studies also show that the catalytic phosphoserine of the missense variants is more stable to hydrolysis relative to wild-type enzyme. The structural perturbation resulting from mutation of this single amino acid reveals the molecular mechanism underlying PGM1 deficiency in these missense variants. DATABASE: Structural data are available in the PDB under the accession numbers 5JN5 and 5TR2.
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