ArticleProtein science : a publication of the Protein Society2016
Substrate channeling between the human dihydrofolate reductase and thymidylate synthase.
Article in Protein science : a publication of the Protein Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 23 citations in OpenAlex.
- Advances in PSMA theranostics.Translational oncology · 2022Article
- Structural insight on assembly-line catalysis in terpene biosynthesis.Nature communications · 2021Article
- Brownian Dynamics Simulations of Biological Molecules.Trends in chemistry · 2019Article
- Markov-State Transition Path Analysis of Electrostatic Channeling.The journal of physical chemistry. C, Nanomaterials and interfaces · 2019Article
- New Insight into the Octamer of TYMS Stabilized by Intermolecular Cys43-Disulfide.International journal of molecular sciences · 2018Article
- Brownian dynamic study of an enzyme metabolon in the TCA cycle: Substrate kinetics and channeling.Protein science : a publication of the Protein Society · 2018Article
- Understanding ligand-receptor non-covalent binding kinetics using molecular modeling.Frontiers in bioscience (Landmark edition) · 2017Review
- Substrate channelling as an approach to cascade reactions.Nature chemistry · 2016Review
- Conservation and Role of Electrostatics in Thymidylate Synthase.Scientific reports · 2015Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
In vivo, as an advanced catalytic strategy, transient non-covalently bound multi-enzyme complexes can be formed to facilitate the relay of substrates, i. e. substrate channeling, between sequential enzymatic reactions and to enhance the throughput of multi-step enzymatic pathways. The human thymidylate synthase and dihydrofolate reductase catalyze two consecutive reactions in the folate metabolism pathway, and experiments have shown that they are very likely to bind in the same multi-enzyme complex in vivo. While reports on the protozoa thymidylate synthase-dihydrofolate reductase bifunctional enzyme give substantial evidences of substrate channeling along a surface "electrostatic highway," attention has not been paid to whether the human thymidylate synthase and dihydrofolate reductase, if they are in contact with each other in the multi-enzyme complex, are capable of substrate channeling employing surface electrostatics. This work utilizes protein-protein docking, electrostatics calculations, and Brownian dynamics to explore the existence and mechanism of the substrate channeling between the human thymidylate synthase and dihydrofolate reductase. The results show that the bound human thymidylate synthase and dihydrofolate reductase are capable of substrate channeling and the formation of the surface "electrostatic highway." The substrate channeling efficiency between the two can be reasonably high and comparable to that of the protozoa.
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Registered trials
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.