Disease relevance of malic acid

• Furthermore, it was distinguished phenotypically from Pseudomonas putida biovar A by utilization of D-malate, L-(+)-tartrate, m-tartrate and nicotinate [1].
• Assimilation of D-malate by Rhodobacter capsulatus E1F1 [2].
• D-Malate dehydrogenase from Escherichia coli does not cross-react with anti-D-malate dehydrogenase to D-malate dehydrogenase form P.fluorescens UK-1 [3].

High impact information on malic acid

• Enzyme kinetics studies confirm that tartrate and the related D-malate are inhibitors of YiaK [4].
• The additional binding sites (sites B) on the other hand also bind the substrates and their analogs D-malate and oxaloacetate, as well as L-aspartate which is not an inhibitor [5].
• 5. The binding of L-malate is promoted at alkaline pH values, whereas the binding of D-malate and hydroxymalonate is favored at acidic pH values [6].
• Data suggest a general base mechanism with likely general acid catalysis in the oxidative decarboxylation of D-malate [7].
• Isocitrate dehydrogenase (IDH) catalyzes the oxidative decarboxylation of isocitrate and has negligible activity toward other (R)-malate-type substrates [8].

Associations of malic acid with other chemical compounds

• Hydroxymalonate and D-malate strongly enhance the fluorescence of the reduced nicotinamide adenine dinucleotide bound to the enzyme [9].
• Six new compounds, diospyrolide (1), diospyrolidone (2), diethyl (2R)-malate (3), 3-(E)-coumaroylbetulin-28-yl ethyl nonanedioate (4), 3-(E)-coumaroylbetulin-28-yl ethyl succinate (5), and 3-(E)-coumaroylbetulin-28-yl ethyl (2R)-2-hydroxysuccinate (6), have been isolated from the heartwood of Diospyros maritima [10].
• D-Malate dehydrogenase was purified to homogeneity from the cells grown on D-malate by using ammonium sulfate precipitation, heat treatment, DEAE-sephadex chromatography, Ultrogel AcA 34 gel filtration and 5'-AMP-Sepharose affinity chromatography [3].

References