ArticleProtein science : a publication of the Protein Society2018
Brownian dynamic study of an enzyme metabolon in the TCA cycle: Substrate kinetics and channeling.
Article in Protein science : a publication of the Protein Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 42 citations in OpenAlex.
- Dynamic assembly of malate dehydrogenase-citrate synthase multienzyme complex in the mitochondria.eLife · 2026Article
- Complete enzyme clustering enhances coenzyme Q biosynthesis via substrate channeling.Nature communications · 2026Article
- Proteomic insights into nano-chitosan-induced salinity tolerance in solid matrix-primed mung bean seedlings.Scientific reports · 2026Article
- Transcriptome-Based Selection and Validation of Reference Genes for Gene Expression Analysis inGenes · 2026Article
- Dynamic Cytoplasm: A Physical Regulator of Enzymatic Function.Biochemistry · 2025Review
- Enzymes in a human cytoplasm model organize into submetabolon complexes.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Acetylation, ADP-ribosylation and methylation of malate dehydrogenase.Essays in biochemistry · 2024Review
- Molecular mechanics studies of factors affecting overall rate in cascade reactions: Multi-enzyme colocalization and environment.Protein science : a publication of the Protein Society · 2024Article
- An Innovative Methodology to Characterize, at the Molecular Scale, Interactions in Polysaccharide Aqueous Solutions.Molecules (Basel, Switzerland) · 2024Article
- On the possibility of the existence of orienting hydrodynamic steering effects in the kinetics of receptor-ligand association.European biophysics journal : EBJ · 2023Review
- The roles of molecular chaperones in regulating cell metabolism.FEBS letters · 2023Review
- The diversity of substrates for plant respiration and how to optimize their use.Plant physiology · 2023Review
- Markov State Study of Electrostatic Channeling within the Tricarboxylic Acid Cycle Supercomplex.ACS nanoscience Au · 2022Article
- Mechanisms and Effects of Substrate Channelling in Enzymatic Cascades.Methods in molecular biology (Clifton, N.J.) · 2022Review
- Investigating Intrinsically Disordered Proteins With Brownian Dynamics.Frontiers in molecular biosciences · 2022Article
- Vectorial channeling as a mechanism for translational control by functional prions and condensates.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Association of the malate dehydrogenase-citrate synthase metabolon is modulated by intermediates of the Krebs tricarboxylic acid cycle.Scientific reports · 2021Article
- Multiscale computational study of ligand binding pathways: Case of p38 MAP kinase and its inhibitors.Biophysical journal · 2021Article
- Metabolic channeling: predictions, deductions, and evidence.Molecular cell · 2021Review
- Co-localization and confinement of ecto-nucleotidases modulate extracellular adenosine nucleotide distributions.PLoS computational biology · 2020Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Malate dehydrogenase (MDH) and citrate synthase (CS) are two pacemaking enzymes involved in the tricarboxylic acid (TCA) cycle. Oxaloacetate (OAA) molecules are the intermediate substrates that are transferred from the MDH to CS to carry out sequential catalysis. It is known that, to achieve a high flux of intermediate transport and reduce the probability of substrate leaking, a MDH-CS metabolon forms to enhance the OAA substrate channeling. In this study, we aim to understand the OAA channeling within possible MDH-CS metabolons that have different structural orientations in their complexes. Three MDH-CS metabolons from native bovine, wild-type porcine, and recombinant sources, published in recent work, were selected to calculate OAA transfer efficiency by Brownian dynamics (BD) simulations and to study, through electrostatic potential calculations, a possible role of charges that drive the substrate channeling. Our results show that an electrostatic channel is formed in the metabolons of native bovine and recombinant porcine enzymes, which guides the oppositely charged OAA molecules passing through the channel and enhances the transfer efficiency. However, the channeling probability in a suggested wild-type porcine metabolon conformation is reduced due to an extended diffusion length between the MDH and CS active sites, implying that the corresponding arrangements of MDH and CS result in the decrease of electrostatic steering between substrates and protein surface and then reduce the substrate transfer efficiency from one active site to another.
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Registered trials
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