Disease relevance of L-Apple acid

• We have expressed the L-lactate dehydrogenase (LDH) and L-malate dehydrogenase (malDH) genes from the apicomplexan Cryptosporidium parvum (CpLDH1 and CpMalDH1) as maltose-binding protein (MBP) fusion proteins in Escherichia coli [1].
• Salmonella typhimurium strains containing a duplication of nearly a third of the genome have been isolated by a simple procedure involving selection for improved utilization of L-malate as sole carbon source [2].
• Electrogenic L-malate transport by Lactobacillus plantarum: a basis for energy derivation from malolactic fermentation [3].
• The proton motive force generated in Leuconostoc oenos by L-malate fermentation [4].
• Repression of sporulation in Bacillus subtilis by L-malate [5].

Psychiatry related information on L-Apple acid

• We investigated in detail the reaction conditions for the simple direct polycondensation of l-malic acid, including the reaction times, temperatures, and catalysts [6].
• The decarboxylation of L-malate in these wines leads to an increase in pH, more organoleptic complexity and microbiological stability [7].

High impact information on L-Apple acid

• Saccharomyces cerevisiae cannot degrade malic acid efficiently due to the lack of a malate transporter and the low substrate affinity of its malic enzyme [8].
• The amino acid sequence of porcine heart mitochondrial malate dehydrogenase (mMDH; L-malate: NAD+ oxidoreductase, EC 1.1.1.37) has been compared with the sequences of six different lactate dehydrogenases (LDH; L-lactate: NAD+ oxidoreductase, EC 1.1.1.27) and with the "x-ray" sequence of cytoplasmic malate dehydrogenase (sMDH) [9].
• By using two substrates, i.e. (S)-malate and 2-hydroxyisobutyrate, the substrate specificity of the mutants was analyzed [10].
• No evidence for substrate-induced expression of mae2 was observed in the presence of 0.2% L-malate [11].
• The NAD-dependent malic enzyme from Schizosaccharomyces pombe catalyzes the oxidative decarboxylation of L-malate to pyruvate and CO2 [11].

Chemical compound and disease context of L-Apple acid

• The fermentation of fumarate and L-malate by Clostridium formicoaceticum was investigated [12].
• H2-dependent anaerobic growth of Escherichia coli on L-malate: succinate formation [13].
• The relationship between the O2 input rate into a suspension of Rhizobium leguminosarum bacteroids, the cellular ATP and ADP pools, and the whole-cell nitrogenase activity during L-malate oxidation has been studied [14].
• An evaluation of the efficiency of the L-alanine and L-malate transport systems was undertaken with the photosynthetic bacterium Rhodospirillum rubrum grown on the amino acid whose uptake was measured [15].
• Membrane vesicles isolated from Bacillus subtilis W23 catalyze active transport of the C4 dicarboxylic acids L-malate, fumarate, and succinate under aerobic conditions in the presence of the electron donor reduced beta-nicotinamide adenine dinucleotide or the non-physiological electron donor system ascorbate-phenazine methosulfate [16].

Biological context of L-Apple acid

• These data are consistent with a previously suggested second "substrate" binding site proposed to explain the enzymatic activation observed at high concentrations of the substrate, L-malate (Telegdi, M., Wolfe, D. V., and Wolfe, R. G. (1973) J. Biol. Chem. 248, 6484-6489) [17].
• The activation of malic enzyme by Mn2+ at high levels of L-malate shows biphasic kinetics yielding two activator constants for Mn2+ [18].
• Similar to other plant PEPCs examined to date, p107 phosphorylation increased PEPC1 activity at pH 7.3 by decreasing its K(m)(PEP) and sensitivity to L-malate inhibition, while enhancing glucose-6-P activation [19].
• The tricarboxylic acid cycle enzyme fumarase (fumarate hydratase; EC 4.2.1.2) catalyzes the reversible hydration of fumarate to L-malate [20].
• In permeabilized cells, the DNA damage generated by AA in combination with either Cf, L-malate or CaCl(2) was blunted by catalase [21].

Anatomical context of L-Apple acid

• ATP (2MM) caused the uptake of 10 nmol of citrate into the mitochondria coincident with the output of a similar amount of L-malate [22].
• The inducible crassulacean acid metabolism (CAM) plant Mesembryanthemum crystallinum accumulates malic acid during the night and converts it to starch during the day via a pathway that, because it is located in different subcellular compartments, depends on specific metabolite transport across membranes [23].
• Electrophysiological studies using the patch-clamp technique were performed on isolated vacuoles from leaf mesophyll cells of the crassulacean acid metabolism (CAM) plant Kalanchoë daigremontiana to characterize the malate transport system responsible for nocturnal malic acid accumulation [24].
• 2. Adenosine triphosphatase, NADH dehydrogenase and L-malate intact protoplasts, but were readily detected in intact stage II or IV forespores, consistent with reversed polarity of the outer forespore membrane relative to the mother-cell plasma membrane [25].
• 2. Methods are described for measurement of incorporation of 32Pi into the complex in rat heart mitochondria oxidizing 2-oxoglutarate + L-malate (total, sites 1, 2 and 3) [26].

Associations of L-Apple acid with other chemical compounds

• In addition to the NAD(P)-dependent oxidative decarboxylation of L-malate, S. solfataricus malic enzyme was able to catalyze the decarboxylation of oxalacetate [27].
• The enzyme showed a strict substrate specificity toward D-quinic acid-related compounds as acceptors; the Km and Vmax values were 16.7 mM and 15.1 units/mg of protein for D-quinic acid, 250 mM and 19.0 units/mg of protein for shikimic acid, and there was no activity with either L-malic acid or meso-tartaric acid [28].
• Branched chain fatty acid beta-oxidation in purified mitochondria was very low, and the oxidation was not stimulated by exogenous L-carnitine or L-malate [29].
• Oxygen-18 incorporation into malic acid during nocturnal carbon dioxide fixation in crassulacean acid metabolism plants. A new approach to estimating in vivo carbonic anhydrase activity [30].
• The pathway of the maloalcoholic fermentation in Schizosaccharomyces pombe was investigated by a 1H-, 2H- and 13C-n.m.r.-spectroscopic study of hydrogen and deuterium distribution on the ethanol produced by S. pombe from L-malic acid in 2H2O and from L-[2-2H]malic acid [31].

Gene context of L-Apple acid

• It was shown to be an NADPH-dependent [lactate dehydrogenase (LDH)-like] L-malate dehydrogenase (MalDH) and not an L-lactate dehydrogenase, as had been suggested previously on the basis of amino acid sequence similarity [32].
• Expression in S. cerevisiae of the MAE1 gene, encoding Schizosaccharomyces pombe malate permease, markedly increased L-malic acid uptake in this yeast [33].
• As found for glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and L-malate dehydrogenase, the relatedness between the archaebacterial aa sequences on the one hand and the eubacterial or eukaryotic sequences on the other is lower than that between the latter ones [34].
• Both the MJ1425-encoded enzyme and the MJ0490-encoded enzyme were found to function to different degrees as malate dehydrogenases, reducing oxalacetate to (S)-malate using either NADH or NADPH as a reductant [35].
• Its Km value for L-malate (1.21 +/- 0.11 mM) is four times higher than that for the natural human breast cancer cell malic enzyme (0.29 +/- 0.04 mM) but similar to that for the full-length recombinant enzyme (1.06 +/- 0.07 mM) [36].

Analytical, diagnostic and therapeutic context of L-Apple acid

• The dissociations of porcine heart mitochondrial, bovine heart mitochondrial, and porcine heart cytoplasmic malate dehydrogenase dimers (L-malate: NAD+oxidoreductase, EC 1.1.1.37) have been examined by Sephadex G-100 gel filtration chromatography and sedimentation velocity ultracentrifugation [37].
• Cytosolic malic enzyme was purified from rat mammary gland by L-malate affinity chromatography [38].
• Direct chiral resolution of malic acid in apple juice by ligand-exchange capillary electrophoresis using copper(II)-L-tartaric acid as a chiral selector [39].
• Fluorescence titration shows that L-malate is also anticooperatively bound in the presence of saturating concentrations of NADH [40].
• Two groups of such mutants, i.e., malic enzyme-deficient and malate transport-defective mutants, were differentiated by a 14C-labeled L-malate transport assay and by starch gel electrophoresis followed by activity staining for malic enzyme (malate dehydrogenase [oxaloacetate decarboxylating] [NAD+]; 1.1.1.38) and malate dehydrogenase (1.1.1.37) [41].

References