ReviewEssays in biochemistry2024
Catalytic mechanism and kinetics of malate dehydrogenase.
Review in Essays in biochemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
8 citing papers in PubMed.
- Article
- Molecular architecture of the human citrate synthase-malate dehydrogenase 2 metabolon.Acta crystallographica. Section D, Structural biology · 2026Article
- Biophysical and enzymatic comparison ofbioRxiv : the preprint server for biology · 2026Article
- Coordinated proteome-scale remodeling underlies polyextremophilic survival in Antarctic cryo-hypersaline brines.Frontiers in microbiology · 2026Article
- Molecular Architecture of the human Citrate Synthase-Malate Dehydrogenase 2 metabolon.bioRxiv : the preprint server for biology · 2025Article
- Measurement of NAD(H) concentration using BCA dye and applications to assays of dehydrogenases.microPublication biology · 2025Article
- Isolation and evaluation of aFrontiers in bioengineering and biotechnology · 2025Article
- The Key Enzymes of Carbon Metabolism and the Glutathione Antioxidant System ProtectJournal of fungi (Basel, Switzerland) · 2024Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Malate dehydrogenase (MDH) is a ubiquitous and central enzyme in cellular metabolism, found in all kingdoms of life, where it plays vital roles in the cytoplasm and various organelles. It catalyzes the reversible NAD+-dependent reduction of L-malate to oxaloacetate. This review describes the reaction mechanism for MDH and the effects of mutations in and around the active site on catalytic activity and substrate specificity, with a particular focus on the loop that encloses the active site after the substrates have bound. While MDH exhibits selectivity for its preferred substrates, mutations can alter the specificity of MDH for each cosubstrate. The kinetic characteristics and similarities of a variety of MDH isozymes are summarized, and they illustrate that the KM values are consistent with the relative concentrations of the substrates in cells. As a result of its existence in different cellular environments, MDH properties vary, making it an attractive model enzyme for studying enzyme activity and structure under different conditions.
Indexed as
Identifiers
What OpenQuestion holds
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.