ArticleBiochemistry2009
Modulation of catalytic function by differential plasticity of the active site: case study of Trypanosoma cruzi trans-sialidase and Trypanosoma rangeli sialidase.
Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 32 citations in OpenAlex.
- Advances and challenges in the search for new treatments for Chagas disease.Memorias do Instituto Oswaldo Cruz · 2026Review
- Molecular Dynamics Simulations Reveal the Conformational Transition of GH33 Sialidases.International journal of molecular sciences · 2023Article
- It All Starts with a Sandwich: Identification of Sialidases with Trans-Glycosylation Activity.PloS one · 2016Article
- Carbohydrate Recognition Specificity of Trans-sialidase Lectin Domain from Trypanosoma congolense.PLoS neglected tropical diseases · 2015Article
- Galactosyl-lactose sialylation using Trypanosoma cruzi trans-sialidase as the biocatalyst and bovine κ-casein-derived glycomacropeptide as the donor substrate.Applied and environmental microbiology · 2014Article
- Unraveling the differences of the hydrolytic activity of Trypanosoma cruzi trans-sialidase and Trypanosoma rangeli sialidase: a quantum mechanics-molecular mechanics modeling study.The journal of physical chemistry. B · 2014Article
- Evidence of ternary complex formation in Trypanosoma cruzi trans-sialidase catalysis.The Journal of biological chemistry · 2014Article
- Design of e-pharmacophore models using compound fragments for the trans-sialidase of Trypanosoma cruzi: screening for novel inhibitor scaffolds.Journal of molecular graphics & modelling · 2013Article
- Insights into the activity and specificity of Trypanosoma cruzi trans-sialidase from molecular dynamics simulations.Biochemistry · 2013Article
- Sialic acid: a sweet swing between mammalian host and Trypanosoma cruzi.Frontiers in immunology · 2012Article
- Proton transfer facilitated by ligand binding. An energetic analysis of the catalytic mechanism of Trypanosoma cruzi trans-sialidase.Biochemistry · 2011Article
- Tryptophan as a molecular shovel in the glycosyl transfer activity of Trypanosoma cruzi trans-sialidase.Biophysical journal · 2010Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
trans-Sialidase is an essential enzyme for Trypanosoma cruzi, the causative agent of Chagas' disease, to escape from the host immune system and to invade the host cells. Therefore, T. cruzi trans-sialidase (TcTS) presents a potential and appealing therapeutic target for this lethal disease. The availability of a structurally very similar enzyme with strict hydrolase activity (Trypanosoma rangeli sialidase, TrSA) provides us a unique opportunity to understand the determinants of their structure and catalytic mechanism. In this study, we compare the catalytic cleft plasticity of free (apo) and ligand-bound (holo) forms of the two enzymes using molecular dynamics simulations. We focus on the mouth of the catalytic cleft that is defined by two residues: W312 and Y119 in TcTS and W312 and S119 in TrSA. Our results indicate that TcTS has a very flexible, widely open catalytic cleft, mostly due to W312 loop motion, in apo form. However, when the catalytic cleft is occupied by a ligand, the flexibility and solvent exposure of TcTS is significantly reduced. On the other hand, TrSA maintains a more open catalytic cleft compared to its crystal structures in both apo and holo forms (and compared to TcTS in holo forms). The reduced solvent exposure of TcTS catalytic cleft might be partially or fully responsible for TcTS to be a less efficient hydrolase than TrSA.
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