Evidence map›Paper›PMID 25849117›Full record

ArticlePLoS computational biology2015

Stepwise catalytic mechanism via short-lived intermediate inferred from combined QM/MM MERP and PES calculations on retaining glycosyltransferase ppGalNAcT2.

Tomáš Trnka, Stanislav Kozmon, Igor Tvaroška, Jaroslav Koča

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Article in PLoS computational biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

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0cells of the map it votes in
7citing papers in PubMed
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1 · What the graph read from it

What it found

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2 · The registry

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3 · Its place in the literature

Who cites it

7 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Article
  6. Review
  7. Polypeptide GalNAc-Ts: from redundancy to specificity.Current opinion in structural biology · 2019
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors.

Tomáš TrnkaCentral European Institute of Technology (CEITEC), Masaryk University, Brno, Czech Republic; Faculty of Science-National Centre for Biomolecular Research, Masaryk University, Brno, Czech Republic.
Stanislav KozmonCentral European Institute of Technology (CEITEC), Masaryk University, Brno, Czech Republic; Faculty of Science-National Centre for Biomolecular Research, Masaryk University, Brno, Czech Republic; On leave from the Institute of Chemistry, Slovak Academy of Sciences, Bratislava, Slovak Republic.
Igor TvaroškaCentral European Institute of Technology (CEITEC), Masaryk University, Brno, Czech Republic; Institute of Chemistry, Slovak Academy of Sciences, Bratislava, Slovak Republic.
Jaroslav KočaCentral European Institute of Technology (CEITEC), Masaryk University, Brno, Czech Republic; Faculty of Science-National Centre for Biomolecular Research, Masaryk University, Brno, Czech Republic.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The glycosylation of cell surface proteins plays a crucial role in a multitude of biological processes, such as cell adhesion and recognition. To understand the process of protein glycosylation, the reaction mechanisms of the participating enzymes need to be known. However, the reaction mechanism of retaining glycosyltransferases has not yet been sufficiently explained. Here we investigated the catalytic mechanism of human isoform 2 of the retaining glycosyltransferase polypeptide UDP-GalNAc transferase by coupling two different QM/MM-based approaches, namely a potential energy surface scan in two distance difference dimensions and a minimum energy reaction path optimisation using the Nudged Elastic Band method. Potential energy scan studies often suffer from inadequate sampling of reactive processes due to a predefined scan coordinate system. At the same time, path optimisation methods enable the sampling of a virtually unlimited number of dimensions, but their results cannot be unambiguously interpreted without knowledge of the potential energy surface. By combining these methods, we have been able to eliminate the most significant sources of potential errors inherent to each of these approaches. The structural model is based on the crystal structure of human isoform 2. In the QM/MM method, the QM region consists of 275 atoms, the remaining 5776 atoms were in the MM region. We found that ppGalNAcT2 catalyzes a same-face nucleophilic substitution with internal return (SNi). The optimized transition state for the reaction is 13.8 kcal/mol higher in energy than the reactant while the energy of the product complex is 6.7 kcal/mol lower. During the process of nucleophilic attack, a proton is synchronously transferred to the leaving phosphate. The presence of a short-lived metastable oxocarbenium intermediate is likely, as indicated by the reaction energy profiles obtained using high-level density functionals.

Indexed as

Models, ChemicalModels, MolecularAlgorithmsBinding SitesCatalysisComputer SimulationGlycosylationGlycosyltransferasesKineticsPolysaccharidesProtein BindingProtein ConformationGlycosyltransferasesPolysaccharides

Identifiers

PMID25849117
PMCPMC4388629

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.