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Related Concept Videos

Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.

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Related Experiment Video

Updated: Jul 9, 2026

Understanding the Development of Compensatory Pathways in a Mutant Malaria Parasite Harbouring Hypomorphic Allele of Plant-Like Kinases
09:13

Understanding the Development of Compensatory Pathways in a Mutant Malaria Parasite Harbouring Hypomorphic Allele of Plant-Like Kinases

Published on: November 22, 2024

Structural insights into mutated human phosphoglucomutase 1 (PGM1) using computational approaches.

Eman Abdullah Almuqri1

  • 1Department of Biology, College of Science, Imam Mohammad Ibn Saud Islamic University (IMSIU), Riyadh, Saudi Arabia.

Journal of Biomolecular Structure & Dynamics
|July 7, 2026
PubMed
Summary
This summary is machine-generated.

Mutations in the phosphoglucomutase 1 (PGM1) enzyme disrupt its structure and stability, impacting metabolism and glycosylation. These PGM1 variants are linked to congenital disorders of glycosylation (CDGs).

Keywords:
Free energy landscapeMD simulationPhosphoglucomutase 1Protein structural stabilityVariants

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In Vitro Enzyme Measurement to Test Pharmacological Chaperone Responsiveness in Fabry and Pompe Disease
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In Vitro Enzyme Measurement to Test Pharmacological Chaperone Responsiveness in Fabry and Pompe Disease

Published on: December 20, 2017

Area of Science:

  • Biochemistry
  • Structural Biology
  • Computational Biology

Background:

  • The phosphoglucomutase 1 (PGM1) enzyme is vital for human metabolism and glycosylation.
  • PGM1 dysfunction is associated with inherited metabolic disorders like congenital disorders of glycosylation (CDGs).
  • Gene mutations can affect PGM1's catalytic activity and protein folding.

Purpose of the Study:

  • To investigate the molecular and structural consequences of specific PGM1 variants (T19A, N38Y, D62H).
  • To analyze the impact of these mutations on protein stability and dynamics at a supramolecular level.

Main Methods:

  • Utilized long-timescale (500 ns) molecular dynamics (MD) simulations.
  • Analyzed key structural parameters including RMSD, RMSF, Rg, SASA, hydrogen bonds, and Free Energy Landscape (FEL).
  • Compared variant PGM1 features against the wild-type enzyme.

Main Results:

  • PGM1 variants T19A, N38Y, and D62H exhibit significantly altered structural behavior compared to wild-type.
  • Mutations lead to increased protein flexibility and reduced stability.
  • Changes in compactness and other dynamic parameters were observed for the studied PGM1 variants.

Conclusions:

  • The studied PGM1 mutations (T19A, N38Y, D62H) destabilize the enzyme.
  • These structural alterations provide molecular insights into PGM1-related metabolic and glycosylation disorders.
  • Understanding these variant effects is crucial for comprehending CDGs pathogenesis.