Journal of Biological Chemistry, 1967 Abstract The apparent pH optimum of oxalacetate reduction by the malate dehydrogenase of Bacillus subtilis changed from pH 9.0 to pH 6.0 during the three crystallizations required to achieve maximal specific activity. The change was apparently due to an alteration in the substrate inhibition characteristics of the enzyme.
William H. Murphey, Nathan O. Kaplan
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Malic Enzyme, not Malate Dehydrogenase, Mainly Oxidizes Malate That Originates from the Tricarboxylic Acid Cycle in Cyanobacteria [PDF]
mBio, 2022 Oxygenic photoautotrophic bacteria, cyanobacteria, have the tricarboxylic acid (TCA) cycle, and metabolite production using the cyanobacterial TCA cycle has been spotlighted recently. The unicellular cyanobacterium Synechocystis sp.
Noriaki Katayama +4 more
doaj +2 more sources
Isoenzymes of Malate Dehydrogenase in Saccharomyces cerevisiae [PDF]
European Journal of Biochemistry, 1968 Extracts from yeast cells grown under different conditions and from mitochondria were subjected to agar gel electrophoresis. Three bands showing malate dehydrogenase activity were found in extracts from aerobic derepressed cells (c‐MDH I, c‐MDH II, and m‐MDH III), whereas generally only one band was present in extracts from anaerobic repressed cells (c‐
W. Atzpodien +3 more
openalex +6 more sources
Determination of acetyl coenzyme A. Interference by a contaminant in malate dehydrogenase
Journal of Lipid Research, 1972 Spectrophotometric determinations of acetyl CoA with malate dehydrogenase and citrate synthase are likely to overestimate the amount of acetyl CoA in solutions containing acetoacetyl CoA, since commercial preparations of malate dehydrogenase may contain ...
I. Mulder
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Enhanced succinic acid production by Mannheimia employing optimal malate dehydrogenase. [PDF]
Nat Commun, 2020 Succinic acid (SA), a dicarboxylic acid of industrial importance, can be efficiently produced by metabolically engineered Mannheimia succiniciproducens.
Ahn JH +8 more
europepmc +2 more sources
Malate dehydrogenase 2 deficiency is an emerging cause of pediatric epileptic encephalopathy with a recognizable biochemical signature [PDF]
Molecular Genetics and Metabolism Reports, 2022 Malate dehydrogenases (MDH) serve a critical role in maintaining equilibrium of the NAD+/NADH ratio between the mitochondria and cytosol through the catalysis of the oxidation of L-malate to oxaloacetate in a reversible, NADH-dependent manner.
Jessica R.C. Priestley +18 more
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Plasmodium Parasite Malate-Quinone Oxidoreductase Functionally Complements a Yeast Deletion Mutant of Mitochondrial Malate Dehydrogenase [PDF]
Microbiology Spectrum, 2023 The emergence of drug-resistant variants of malaria-causing Plasmodium parasites is a life-threatening problem worldwide. Investigation of the physiological function of individual parasite proteins is a prerequisite for a deeper understanding of the ...
Takeshi Ito +3 more
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Studying the Lysine Acetylation of Malate Dehydrogenase. [PDF]
Journal of Molecular Biology, 2017 Protein acetylation plays important roles in many biological processes. Malate dehydrogenase (MDH), a key enzyme in the tricarboxylic acid cycle, has been identified to be acetylated in bacteria by proteomic studies, but no further characterization has been reported. One challenge for studying protein acetylation is to get purely acetylated proteins at
Suryawanshi Venkat Shivaji +4 more
semanticscholar +4 more sources
Catalytic mechanism and kinetics of malate dehydrogenase. [PDF]
Essays BiochemAbstract 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.
de Lorenzo L +3 more
europepmc +3 more sources
Induced pluripotent stem cell-derived hepatocytes reveal TCA cycle disruption and the potential basis for triheptanoin treatment for malate dehydrogenase 2 deficiency [PDF]
Molecular Genetics and Metabolism ReportsMitochondrial malate dehydrogenase 2 (MDH2) is crucial to cellular energy generation through direct participation in the tricarboxylic acid (TCA) cycle and the malate aspartate shuttle (MAS).
Déborah Mathis +8 more
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