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1. Full Text Mitochondrial malic enzyme (ME2) in pancreatic islets of the human, rat and mouse and clonal insulinoma cells. Simple enzyme assay for mitochondrial malic enzyme 2
by MacDonald, Michael J and Longacre, Melissa J and Kendrick, Mindy A
Archives of Biochemistry and Biophysics, ISSN 0003-9861, 08/2009, Volume 488, Issue 2, pp. 100 - 104
Despite interest in malic enzyme(ME)s in insulin cells, mitochondrial malic enzyme (ME2) has only been studied with estimates of mRNA or with mRNA knockdown.... 
Fumarate activation | ATP inhibition | Malate | Spectrophotometric enzyme assay procedure | Mitochondrial NAD(P) malic enzyme | Pancreatic islets | ME2 | PATHWAYS | ISOFORMS | FEASIBILITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | PHOSPHOENOLPYRUVATE CARBOXYKINASE | BIOPHYSICS | PYRUVATE-KINASE | GLYCEROL PHOSPHATE DEHYDROGENASE | GLUCOSE-METABOLISM | BETA-CELL | SECRETION | NMR ISOTOPOMER ANALYSIS | malate | spectrophotometric enzyme assay procedure | pancreatic islets | fumarate activation
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2. Full Text Expression of cytosolic malic enzyme (ME1) is associated with disease progression in human oral squamous cell carcinoma
by Nakashima, Chie and Yamamoto, Kazuhiko and Fujiwara‐Tani, Rina and Luo, Yi and Matsushima, Sayako and Fujii, Kiyomu and Ohmori, Hitoshi and Sasahira, Tomonori and Sasaki, Takamitsu and Kitadai, Yasuhiko and Kirita, Tadaaki and Kuniyasu, Hiroki
Cancer Science, ISSN 1347-9032, 06/2018, Volume 109, Issue 6, pp. 2036 - 2045
Malic enzyme 1 (ME1) is a multifunctional protein involved in glycolysis, the citric acid cycle, NADPH production, glutamine metabolism, and lipogenesis. It is... 
malic enzyme | cancer invasion | glutamine | prognosis | stemness | HEAD | CANCER CELLS | MECHANISM | EPITHELIAL-MESENCHYMAL TRANSITION | INHIBITION | METABOLISM | ONCOLOGY | GROWTH | SENESCENCE | NECK | Immunohistochemistry | Lactates | Glucose metabolism | Enzymes | Squamous cell carcinoma | Analysis | Development and progression | Fermentation | Glutamine | Cell proliferation | Tricarboxylic acid cycle | Energy metabolism | Phosphorylation | Dehydrogenases | Mesenchyme | Amino acids | Kinases | Cancer therapies | Cell adhesion & migration | Mitochondria | Cell growth | Feedback | Conflicts of interest | NADP | Lipogenesis | Personal information | Oral carcinoma | Oral squamous cell carcinoma | Citric acid | Malic enzyme | Oxidative phosphorylation | Medical prognosis | Glycolysis | Lactic acid | Tumors | Original
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3. Full Text Increasing lipid production using an NADP+-dependent malic enzyme from Rhodococcus jostii
by Hernández, Martín A and Alvarez, Héctor M
Microbiology (Reading, England), ISSN 1350-0872, 01/2019, Volume 165, Issue 1, pp. 4 - 14
The occurrence of NADP(+)-dependent malic enzymes (NADP(+)-MEs) in several Rhodococcus strains was analysed. The NADP(+)-ME number in Rhodococcus genomes... 
Rhodococcus | triacylglycerols | malic enzyme | NADP | TRIACYLGLYCEROL BIOSYNTHESIS | YARROWIA-LIPOLYTICA | OPACUS PD630 | CRUDE GLYCEROL | STORAGE LIPIDS | MICROBIOLOGY | MUCOR-CIRCINELLOIDES | NADP(+) | FATTY-ACID | BIODIESEL | ACCUMULATION | OLEAGINOUS MICROORGANISMS
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4. Full Text Functional Roles of Metabolic Intermediates in Regulating the Human Mitochondrial NAD(P)+-Dependent Malic Enzyme
by Hsieh, Ju-Yi and Shih, Wan-Ting and Kuo, Yu-Hsuan and Liu, Guang-Yaw and Hung, Hui-Chih
Scientific Reports, ISSN 2045-2322, 12/2019, Volume 9, Issue 1, pp. 9081 - 14
Human mitochondrial NAD(P)(+)-dependent malic enzyme (m-NAD(P)-ME) has a dimer of dimers quaternary structure with two independent allosteric sites in each... 
ANALYTICAL ULTRACENTRIFUGATION | MALATE | SUBSTRATE | GLUTAMATE | MULTIDISCIPLINARY SCIENCES | STATE | SIZE-DISTRIBUTION ANALYSIS | ATP | BINDING | EXPRESSION | PROGRESSION | Enzymes | Size distribution | Nucleotides | Monomers | Malic enzyme | Intermediates | NAD | Mitochondria | Allosteric properties | Mutagenesis | Site-directed mutagenesis | Quaternary structure | Ligands | Catalysis | Protein structure
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5. Full Text The crystal structure of the malic enzyme from Candidatus Phytoplasma reveals the minimal structural determinants for a malic enzyme
by Alvarez, C. E and Trajtenberg, F and Larrieux, N and Saigo, M and Golic, A and Andreo, C. S and Hogenhout, S. A and Mussi, M. A and Drincovich, M. F and Buschiazzo, A
Acta Crystallographica Section D, ISSN 2059-7983, 04/2018, Volume 74, Issue 4, pp. 332 - 340
Phytoplasmas are wall‐less phytopathogenic bacteria that produce devastating effects in a wide variety of plants. Reductive evolution has shaped their genome,... 
crystallography | aster yellows | Candidatus Phytoplasma | phytoplasma | plant pathogens | malic enzyme | reductive metabolism | AYWB | homodimer | Aster yellows | Homodimer | Reductive metabolism | Crystallography | Plant pathogens | Malic enzyme | Phytoplasma | CATALYSIS | ISOFORMS | ZEA-MAYS | MALATE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | BIOCHEMICAL RESEARCH METHODS | IDENTIFICATION | BIOPHYSICS | METABOLIC-REGULATION | DIVERSITY | EXPRESSION | BINDING | Phytoplasma - enzymology | Bacterial Proteins - chemistry | Catalytic Domain - genetics | Crystallography, X-Ray | Protein Conformation | Malate Dehydrogenase - chemistry | Phylogeny | Dimerization | Enzymes | Biological evolution | Evolutionary genetics | Catalytic activity | Genomes | Enzymatic activity | Malate | Decarboxylation | Yellows | Catalysis | Witches' broom | Crystal structure | Cassettes
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6. Full Text Comparative effect of indomethacin (IndoM) on the enzymes of carbohydrate metabolism, brush border membrane and oxidative stress in the kidney, small intestine and liver of rats
by Khan, Sheeba and Yusufi, Faiz Noor Khan and Yusufi, Ahad Noor Khan
Toxicology Reports, ISSN 2214-7500, 2019, Volume 6, pp. 389 - 394
Indomethacin (IndoM) has prominent anti-inflammatory and analgesic-antipyretic properties. However, high incidence and severity of side-effects on the... 
Oxidative stress | Intestine | Toxicity | Liver | Carbohydrate metabolism | Indomethacin | Kidney
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7. Full Text Directed evolution of thermotolerant malic enzyme for improved malate production
by Morimoto, Yumi and Honda, Kohsuke and Ye, Xiaoting and Okano, Kenji and Ohtake, Hisao
Journal of Bioscience and Bioengineering, ISSN 1389-1723, 02/2014, Volume 117, Issue 2, pp. 147 - 152
The directed evolution of the thermotolerant NADP(H)-dependent malic enzyme from was conducted to alter the cofactor preference of the enzyme from NADP(H) to... 
Directed evolution | Reaction specificity | Cofactor preference | [formula omitted] fixation | Malic enzyme | fixation | HCO | COENZYME | ACID | MECHANISM | CONVERSION | REGENERATION | FOOD SCIENCE & TECHNOLOGY | HCO3- fixation | PATHWAY | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | CARBON-DIOXIDE | FIXATION | PIGEON | Malate Dehydrogenase - metabolism | Biocatalysis | Gene Library | Oxidation-Reduction | Substrate Specificity | Directed Molecular Evolution | Enzyme Assays | Malate Dehydrogenase - genetics | Point Mutation - genetics | Thermococcus - enzymology | Malates - metabolism | Protein Engineering | Pyruvic Acid - metabolism | Kinetics | Malate Dehydrogenase - chemistry | NADP - metabolism | NAD - metabolism | Lactates | Enzymes | Gene mutations | Analysis
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8. Full Text Effective Artificial Co-enzyme Based on Single-Electron Reduced Form of 2,2′-Bipyridinium Salt Derivatives for Formate Dehydrogenase in the Catalytic Conversion of CO2 to Formic Acid
by Ikeyama, Shusaku and Abe, Ryutaro and Shiotani, Sachina and Amao, Yutaka
Bulletin of the Chemical Society of Japan, ISSN 0009-2673, 9/2018, Volume 91, Issue 9, pp. 1369 - 1376
Formate dehydrogenase (FDH) is a useful biocatalyst for CO2 reduction to formic acid in a photoredox system consisting of a photosensitizer and an electron... 
Formate dehydrogenase (FDH) | reduction | Artificial co-enzyme | SOLUBLE ZINC PORPHYRIN | SYSTEM | WATER OXIDATION | CANDIDA-BOIDINII | CHEMISTRY, MULTIDISCIPLINARY | PHOTOELECTROCHEMICAL REDUCTION | VISIBLE-LIGHT | MALIC ENZYME | TRANSFER COMMUNICATION | CO2 reduction | PROPYLENE-OXIDE | CARBON-DIOXIDE | Enzymes | Reduction | Dehydrogenases | Formic acid | Carbon dioxide | Nicotinamide adenine dinucleotide | Catalytic activity | Formate dehydrogenase | Catalytic converters | Single electrons
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9. Full Text A Three‐Enzyme Pathway with an Optimised Geometric Arrangement to Facilitate Substrate Transfer
by Liu, Minghui and Fu, Jinglin and Qi, Xiaodong and Wootten, Shaun and Woodbury, Neal W and Liu, Yan and Yan, Hao
ChemBioChem, ISSN 1439-4227, 06/2016, Volume 17, Issue 12, pp. 1097 - 1101
Cascade reactions drive and regulate a variety of metabolic activities. Efficient coupling of substrate transport between enzymes is important for overall... 
self-assembly | DNA nanostructures | malic dehydrogenase | enzyme cascade | Malic dehydrogenase | Self-assembly | Enzyme cascade | CHEMISTRY, MEDICINAL | ORIGAMI | MALATE-DEHYDROGENASE | MOLECULE | BIOCHEMISTRY & MOLECULAR BIOLOGY | COMPLEXES | ARRAYS | ENZYME | SCAFFOLDS | NANOWIRES | LATTICE | Enzymes - chemistry | L-Lactate Dehydrogenase - metabolism | Malate Dehydrogenase - metabolism | Oxidation-Reduction | Substrate Specificity | Carboxy-Lyases - chemistry | DNA - metabolism | Thermodynamics | DNA - chemistry | L-Lactate Dehydrogenase - chemistry | Nanostructures - chemistry | Carboxy-Lyases - metabolism | Malate Dehydrogenase - chemistry | Enzymes - metabolism | Genetic research | Enzymes
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10. Full Text Superior aluminium (Al) tolerance of Stylosanthes is achieved mainly by malate synthesis through an Al-enhanced malic enzyme, SgME1
by Lili Sun and Cuiyue Liang and Zhijian Chen and Pandao Liu and Jiang Tian and Guodao Liu and Hong Liao
New Phytologist, ISSN 0028-646X, 4/2014, Volume 202, Issue 1, pp. 209 - 219
(stylo) is a dominant leguminous forage in the tropics. Previous studies suggest that stylo has great potential for aluminium (Al) tolerance, but little is... 
Yeasts | Aluminum | Full Papers | Root growth | Plant roots | Exudation | Plants | Transgenic plants | Genotypes | Organic acids | Rice | aluminium (Al) tolerance | malate exudation | malic enzyme | malate synthesis | Stylosanthes | Malate synthesis | Aluminium (Al) tolerance | Malate exudation | Malic enzyme | ARABIDOPSIS-THALIANA | PHOSPHORUS EFFICIENCY | ORGANIC-ACIDS | PLASMA-MEMBRANE | ACID SOILS | PLANT SCIENCES | CELL-WALL | RICE CULTIVARS | RESISTANCE | INTERNAL DETOXIFICATION | PHASEOLUS-VULGARIS | Malate Dehydrogenase - metabolism | Arabidopsis - physiology | Saccharomyces cerevisiae - physiology | Arabidopsis - drug effects | Adaptation, Physiological - drug effects | Malate Dehydrogenase - isolation & purification | Oryza - physiology | Plant Exudates - metabolism | Electrophoresis, Gel, Two-Dimensional | Genotype | Saccharomyces cerevisiae - drug effects | Aluminum - toxicity | Oryza - drug effects | Plant Roots - drug effects | Arabidopsis - genetics | Phenotype | Plants, Genetically Modified | Malates - metabolism | Fabaceae - drug effects | Fabaceae - enzymology | Fabaceae - genetics | Fabaceae - physiology | Plant Roots - growth & development | Arabidopsis thaliana | Enzymes | Analysis | Genes | Index Medicus
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11. Full Text Long-range interaction between the enzyme active site and a distant allosteric site in the human mitochondrial NAD(P) +-dependent malic enzyme
by Hsieh, Ju-Yi and Su, Kuo-Liang and Ho, Pei-Tzu and Hung, Hui-Chih
Archives of Biochemistry and Biophysics, ISSN 0003-9861, 2009, Volume 487, Issue 1, pp. 19 - 27
Our previous study has suggested that mutation of the amino acid residue Asp102 has a significant effect on the fumarate-mediated activation of human... 
Coupling energy | Double-mutant cycle | Mutagenesis | Allosteric regulation | Binding energy | Enzyme kinetics | Malic enzyme | Free energy | ANALYTICAL ULTRACENTRIFUGATION | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | FUNCTIONAL-ROLE | NAD | BIOPHYSICS | MN2+-L-MALATE BINDING | PURIFICATION | CATALYTIC MECHANISM | CDNA CLONING | ASCARIS-SUUM | OXIDATIVE DECARBOXYLASES | Mitochondria - enzymology | Humans | Molecular Sequence Data | DNA Primers - genetics | Malate Dehydrogenase - genetics | Thermodynamics | Base Sequence | Allosteric Site - genetics | Malate Dehydrogenase - metabolism | Recombinant Proteins - metabolism | Amino Acid Sequence | Mutagenesis, Site-Directed | Catalytic Domain - genetics | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Static Electricity | Arginine - chemistry | Sequence Homology, Amino Acid | Fumarates - metabolism | Aspartic Acid - chemistry | Kinetics | Malate Dehydrogenase - chemistry | In Vitro Techniques | Amino Acid Substitution | Index Medicus
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12. Full Text Modelling as a tool of enzyme reaction engineering for enzyme reactor development
by Vasić-Rački, Durda and Findrik, Zvjezdana and Vrsalović Presečki, Ana
Applied Microbiology and Biotechnology, ISSN 0175-7598, 8/2011, Volume 91, Issue 4, pp. 845 - 856
Strategy of the development of model for enzyme reactor at laboratory scale with respect to the modelling of kinetics is presented. The recent literature on... 
Biotechnology | Chemistry | Microbiology | Enzyme reactor development | Microbial Genetics and Genomics | Development of biocatalytic reaction | Modelling of enzyme kinetics | Enzyme kinetics | PARAMETER-ESTIMATION | KINETIC-MODEL | MALIC ACID PRODUCTION | CATALYZED ESTERIFICATION | SIMULATION | NADH OXIDASE | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | LACTOBACILLUS-BREVIS | SENSITIVITY-ANALYSIS | OPTIMIZATION | THERMAL INACTIVATION | Models, Theoretical | Biotechnology - methods | Kinetics | Models, Chemical | Bioreactors | Enzymes - metabolism | Enzymes | Universities and colleges | Studies | Catalysis | Chemical reactors | Analysis
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13. Full Text Inside Cover: A Three‐Enzyme Pathway with an Optimised Geometric Arrangement to Facilitate Substrate Transfer (ChemBioChem 12/2016)
by Liu, Minghui and Fu, Jinglin and Qi, Xiaodong and Wootten, Shaun and Woodbury, Neal W and Liu, Yan and Yan, Hao
ChemBioChem, ISSN 1439-4227, 06/2016, Volume 17, Issue 12, pp. 1045 - 1045
The inside cover picture shows the efficient coupling of substrate transport between enzymes, which is important for the overall activity of the pathway. This... 
self-assembly | DNA nanostructures | malic dehydrogenase | enzyme cascade
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14. Full Text Effect of malic enzyme on ethanol production by Synechocystis sp. PCC 6803
by Yoshikawa, Katsunori and Hirasawa, Takashi and Shimizu, Hiroshi
Journal of Bioscience and Bioengineering, ISSN 1389-1723, 01/2015, Volume 119, Issue 1, pp. 82 - 84
We investigated effects of malic enzyme on ethanol production by sp. PCC 6803 under autotrophic conditions. Deletion of , which encodes malic enzyme, decreased... 
Bioproduction | Ethanol | Synechocystis sp. PCC 6803 | Malic enzyme | Cyanobacteria | BIOTECHNOLOGY | METABOLISM | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | FOOD SCIENCE & TECHNOLOGY | Synechocystis sp PCC 6803 | CARBON-DIOXIDE | Malate Dehydrogenase - metabolism | Ethanol - metabolism | Synechocystis - metabolism | Enzymes | Alcohol | Alcohol, Denatured | Evolutionary biology | Production data | Information science
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15. Full Text The effect of NADP‐dependent malic enzyme expression and anaerobic C4 metabolism in Escherichia coli compared with other anaplerotic enzymes
by Kwon, Y.‐D and Kwon, O.‐H and Lee, H.‐S and Kim, P
Journal of Applied Microbiology, ISSN 1364-5072, 12/2007, Volume 103, Issue 6, pp. 2340 - 2345
Aims:  To understand the modification of C4‐metabolism under anaerobic glycolysis condition by overexpressing anaplerotic enzymes, which mediating... 
C4 metabolism | NADP‐dependent malic enzyme | anaplerotic enzymes | Escherichia coli | NADP-dependent malic enzyme | Anaplerotic enzymes | MUTANT | PHOSPHOENOLPYRUVATE CARBOXYLASE | MICROBIOLOGY | CARBOXYKINASE | OVEREXPRESSION | PYRUVATE-CARBOXYLASE | PATHWAY | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | FERMENTATION | SUCCINIC ACID PRODUCTION | Anaerobiosis | Malate Dehydrogenase - metabolism | Carbon - metabolism | Industrial Microbiology | Carbon Dioxide - metabolism | Phosphoenolpyruvate Carboxylase - analysis | Malate Dehydrogenase (NADP+) - genetics | Sodium Bicarbonate - pharmacology | Electroporation | Phosphoenolpyruvate Carboxylase - genetics | Malate Dehydrogenase - genetics | Phosphoenolpyruvate Carboxykinase (ATP) - analysis | Polymerase Chain Reaction - methods | Phosphoenolpyruvate Carboxykinase (ATP) - genetics | Malate Dehydrogenase (NADP+) - metabolism | Escherichia coli - genetics | Malate Dehydrogenase - analysis | Phosphoenolpyruvate Carboxykinase (ATP) - metabolism | Phosphoenolpyruvate Carboxylase - metabolism | Escherichia coli - metabolism | Sodium Bicarbonate - metabolism | Glycolysis | Plasmids - administration & dosage | Physiological aspects | Glucose metabolism | Enzymes | Metabolites | Comparative analysis
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16. Full Text Malic Enzyme 1 (ME1) is pro-oncogenic in ApcMin/+ mice
by Fernandes, Lorenzo M and Al-Dwairi, Ahmed and Simmen, Rosalia C. M and Marji, Meera and Brown, Dustin M and Jewell, Sarah W and Simmen, Frank A
Scientific Reports, ISSN 2045-2322, 12/2018, Volume 8, Issue 1, pp. 1 - 14
Cytosolic Malic Enzyme (ME1) provides reduced NADP for anabolism and maintenance of redox status. To examine the role of ME1 in tumor genesis of the... 
Enzymes | Wnt protein | Epithelial cells | Lamina propria | Villus | mRNA | Gastrointestinal tract | Adenoma | Epithelium | Small intestine | Ileum | Malic enzyme | β-catenin | Jejunum | Rodents | NADP | Tumors
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