ArticleBiophysical journal2015
Determination of the catalytic mechanism for mitochondrial malate dehydrogenase.
Article in Biophysical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 35 citations in OpenAlex.
- Lactate dehydrogenase A exhibits sorbitol/fructose-related catalytic activity and contributes to polyol pathway metabolism in tumor cells.Frontiers in endocrinology · 2026Article
- 2-Hydroxyglutarate in onco-pathway: a metabolic driver of proto-oncogene activation.Frontiers in oncology · 2026Review
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- Enzymes helping enzymes: Oxaloacetate decarboxylase increases malate dehydrogenase's turnover number.PNAS nexus · 2025Article
- Catalytic mechanism and kinetics of malate dehydrogenase.Essays in biochemistry · 2024Review
- Roles ofFrontiers in physiology · 2023Article
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- Salivary Glands after Prolonged Aluminum Exposure: Proteomic Approach Underlying Biochemical and Morphological Impairments in Rats.International journal of molecular sciences · 2022Article
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- A human pluripotent stem cell model for the analysis of metabolic dysfunction in hepatic steatosis.iScience · 2021Article
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- Proteomic analyses unraveling water stress response in two Eucalyptus species originating from contrasting environments for aridity.Molecular biology reports · 2020Article
- Potential biomarkers in septic shock besides lactate.Experimental biology and medicine (Maywood, N.J.) · 2020Review
- Enhanced succinic acid production by Mannheimia employing optimal malate dehydrogenase.Nature communications · 2020Article
- Low Bioavailability and High Immunogenicity of a New Brand of E. colil-Asparaginase with Active Host Contaminating Proteins.EBioMedicine · 2018Article
- Characterization of the kinetics of cardiac cytosolic malate dehydrogenase and comparative analysis of cytosolic and mitochondrial isoforms.Biophysical journal · 2015Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The kinetics of malate dehydrogenase (MDH) catalyzed oxidation/reduction of L-malate/oxaloacetate is pH-dependent due to the proton generated/taken up during the reaction. Previous kinetic studies on the mitochondrial MDH did not yield a consensus kinetic model that explains both substrate and pH dependency of the initial velocity. In this study, we propose, to our knowledge, a new kinetic mechanism to explain kinetic data acquired over a range of pH and substrate concentrations. Progress curves in the forward and reverse reaction directions were obtained under a variety of reactant concentrations to identify associated kinetic parameters. Experiments were conducted at physiologically relevant ionic strength of 0.17 M, pH ranging between 6.5 and 9.0, and at 25 °C. The developed model was built on the prior observation of proton uptake upon binding of NADH to MDH, and that the MDH-catalyzed oxidation of NADH may follow an ordered bi-bi mechanism with NADH/NAD binding to the enzyme first, followed by the binding of oxaloacetate/L-malate. This basic mechanism was expanded to account for additional ionic states to explain the pH dependency of the kinetic behavior, resulting in what we believe to be the first kinetic model explaining both substrate and pH dependency of the reaction velocity.
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