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evolution
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the five PtNADP-ME isoforms cluster in a phylogenetic tree constructed with the whole set of plant NADP-ME sequences, classification into four groups. PtNADP-ME2 and PtNADPME3 cluster with the cytosolic dicot NADP-ME group (group II), while PtNADP-ME4 and PtNADP-ME5 are included in the plastidic dicot NADP-ME group (group III). The group IV comprises both monocot and dicot enzymes, including PtNADP-ME1. Neither of the PtNADP-ME isoforms is included in the monocot NADPMEs (group I)
evolution
the enzyme belongs to the malic superfamily and the NAD_bind_amino_acid_DH superfamily which is a member of the Rossmann fold superfamily
evolution
the enzyme belongs to the malic superfamily and the NAD_bind_amino_acid_DH superfamily which is a member of the Rossmann fold superfamily
evolution
the enzyme belongs to the malic superfamily and the NAD_bind_amino_acid_DH superfamily which is a member of the Rossmann fold superfamily
evolution
the enzyme belongs to the malic superfamily and the NAD_bind_amino_acid_DH superfamily which is a member of the Rossmann fold superfamily
evolution
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the enzyme belongs to the malic superfamily and the NAD_bind_amino_acid_DH superfamily which is a member of the Rossmann fold superfamily
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evolution
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the enzyme belongs to the malic superfamily and the NAD_bind_amino_acid_DH superfamily which is a member of the Rossmann fold superfamily
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malfunction
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antisense reduction of NADP-ME alters C3-C4 cycle coordination. Increase in Rubisco and phosphoenolpyruvate carboxylase activity and leaf nitrogen in low-NADP-ME antisense plants
malfunction
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loss of cytosolic NADP-malic enzyme 2 in Arabidopsis thaliana is associated with enhanced susceptibility to Colletotrichum higginsianum, transient apoplastic reactive oxygen species production after elicitation and callose papilla formation after infection are dampened in mutant nadp-me2
malfunction
the double Sco2951 Sco5261 mutant, deficient in ME-NAD, EC 1.1.1.39, and ME-NADP activity, display a strong reduction in the production of the polyketide antibiotic actinorhodin. Additionally, the Sco2951/Sco5261 mutant shows a decrease in stored triacylglcerides during exponential growth
malfunction
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deletion of the enzyme gene in a Magnaporthe oryzae-resistant rice cultivar disrupts innate immunity against the rice blast fungus
malfunction
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down-regulation of isoform ME2 reciprocally activates p53 through distinct Mdm2 and AMP-activated kinase -mediated mechanisms in a feed-forward manner, bolstering this pathway and enhancing p53 activation. Down-regulation of isoform ME2 also modulates the outcome of p53 activation leading to strong induction of senescence, but not apoptosis
malfunction
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knockdown of malic enzyme 2 suppresses lung tumor growth, induces differentiation and impacts PI3K/AKT signaling. In the A-549 non-small cell lung cancer cell line, ME2 depletion inhibits cell proliferation and induces cell death and differentiation, accompanied by increased reactive oxygen species (ROS) and NADP1/NADPH ratio, a drop in ATP, and increased sensitivity to cisplatin. ME2 knockdown impacts phosphoinositide-dependent protein kinase 1 (PDK1) and phosphatase and tensin homolog (PTEN) expression, leading to AKT inhibition. Depletion of ME2 leads to malate accumulation and pyruvate decrease, and exogenous cell permeable dimethyl-malate mimics the ME2 knockdown phenotype. Both ME2 knockdown and dimethyl-malate treatment reduce A-549 cell growth in vivo. Survival of ME2 knockdown cells is exquisitely dependent on glucose. Phenotype, overview
malfunction
knockdown of ME3, but not ME1 or ME2 (both EC 1.1.1.39) alone or together, inhibits insulin release stimulated by glucose, pyruvate or 2-aminobicyclo [2,2,1]heptane-2-carboxylic acid-plus-glutamine
malfunction
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the decrease of malic enzyme activity is consistent with the cease of lipid accumulation. Reduction of malic enzyme activity is not due to the downregulation of malic enzyme but the feedback repression after nitrogen starvation. Malic enzyme activity recovered by adding ammonium tartrate even at a high cyclohexamide concentration
malfunction
the deprivation of malic enzyme activity limited the lipid accumulation
malfunction
enzyme inactivation improves the anaerobic production of four-carbon dicarboxylic acids by recombinant Escherichia coli strains expressing oxaloacetate-forming pyruvate carboxylase
malfunction
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seeds of Arabidopsis thaliana lacking a functional enzyme isoform NADP-ME1 have reduced seed viability relative to the wild type. Seeds of the loss-of-function mutant display higher levels of protein carbonylation than those of the wild type
malfunction
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seeds of isoform nadp-me1 mutant are less sensitive to the abscisic acid repression of germination and loss viability more rapidly than wild type
malfunction
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suppressing increased enzyme expression in hypertrophied rat hearts reduces pyruvate carboxylation thereby normalizing anaplerosis, restoring GSH content, and reducing lactate accumulation. Reducing the enzyme induces favorable metabolic shifts for carbohydrate oxidation, improving intracellular redox state and enhanced cardiac performance in pathological hypertrophy
malfunction
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the decrease of malic enzyme activity is consistent with the cease of lipid accumulation. Reduction of malic enzyme activity is not due to the downregulation of malic enzyme but the feedback repression after nitrogen starvation. Malic enzyme activity recovered by adding ammonium tartrate even at a high cyclohexamide concentration
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malfunction
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the deprivation of malic enzyme activity limited the lipid accumulation
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malfunction
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the double Sco2951 Sco5261 mutant, deficient in ME-NAD, EC 1.1.1.39, and ME-NADP activity, display a strong reduction in the production of the polyketide antibiotic actinorhodin. Additionally, the Sco2951/Sco5261 mutant shows a decrease in stored triacylglcerides during exponential growth
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metabolism
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the citrate-malate-pyruvate cycle serves to regenerate NAD+ and maintain glycolytic flux. Pyruvate cycles all lead to the exchange of reducing equivalents from mitochondrial NADH to cytosolic NADPH. Malic enzyme is integral to the coupling of metabolism with insulin secretion
metabolism
the enzyme is involved in the fatty acid biosynthesis
metabolism
isoform C4-NADP-ME involved in C4 photosynthesis is modulated by redox status, and its oxidation produces a conformational change limiting the catalytic process, although inducing higher affinity binding of the substrates. Residues Cys192, Cys246, Cys270 and Cys410 are directly or indirectly implicated in C4-NADP-ME redox modulation
metabolism
the enzyme plays a role during fatty acid synthesis
metabolism
during adipocyte differentiation, there is coordinate upregulation of ATP citrate lyase and cytosolic malic enzyme (ME1), which together with cytosolic malate dehydrogenase and at the expense of 1 ATP molecule, can convert citrate and NADH into acetyl-CoA, NADPH and pyruvate
metabolism
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fish spermatozoa contain a glycolytic pathway, tricarboxylic acid cycle and oxidative phosphorylation system, all of which are key pathways contributing to ATP synthesis, involving the enzyme
metabolism
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fish spermatozoa contain a glycolytic pathway, tricarboxylic acid cycle and oxidative phosphorylation system, all of which are key pathways contributing to ATP synthesis, involving the enzyme
metabolism
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fish spermatozoa contain a glycolytic pathway, tricarboxylic acid cycle and oxidative phosphorylation system, all of which are key pathways contributing to ATP synthesis, involving the enzyme
metabolism
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fish spermatozoa contain a glycolytic pathway, tricarboxylic acid cycle and oxidative phosphorylation system, all of which are key pathways contributing to ATP synthesis, involving the enzyme
metabolism
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fish spermatozoa contain a glycolytic pathway, tricarboxylic acid cycle and oxidative phosphorylation system, all of which are key pathways contributing to ATP synthesis, involving the enzyme
metabolism
the enzyme is involved in the transhydrogenase cycle, overview. In view of NADPH as the requisite reducing power in lipid production, the stability of malic enzyme is therefore crucial and malic enzyme activity is significant in the regulation of lipid accumulation
metabolism
the enzyme is involved in the transhydrogenase cycle, overview. In view of NADPH as the requisite reducing power in lipid production, the stability of malic enzyme is therefore crucial and malic enzyme activity is significant in the regulation of lipid accumulation
metabolism
the enzyme is involved in the transhydrogenase cycle, overview. In view of NADPH as the requisite reducing power in lipid production, the stability of malic enzyme is therefore crucial and malic enzyme activity is significant in the regulation of lipid accumulation
metabolism
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the enzyme is involved in the transhydrogenase cycle, overview. In view of NADPH as the requisite reducing power in lipid production, the stability of malic enzyme is therefore crucial and malic enzyme activity is significant in the regulation of lipid accumulation
metabolism
the enzyme is involved in the transhydrogenase cycle, overview. In view of NADPH as the requisite reducing power in lipid production, the stability of malic enzyme is therefore crucial and malic enzyme activity is significant in the regulation of lipid accumulation. The enzyme serves as the sole source of NADPH for fatty acid biosynthesis
metabolism
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the enzyme metabolizes malate, which is important for stabilizing cytoplasmic pH, controlling stomatal aperture, increasing resistance to aluminum excess and pathogens. Pyruvate, another product of the enzyme reaction, participates in the synthesis of defense compounds such as flavonoids and lignin, which are involved in stresses tolerance such as mechanical wounding and pathogen invasion. Moreover, the enzyme provides essential reductive coenzyme NADPH in the biosynthesis of flavonoids and lignin. On the other hand, NADPH is crucial for reactive oxygen species metabolizing systems such as the ascorbate-glutathione pathway and NADPH-dependent thioredoxin reductase, and is also required by apoplastic oxidative burst in most plant-pathogen interactions
metabolism
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the enzyme plays a role during fatty acid synthesis
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metabolism
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the enzyme is involved in the transhydrogenase cycle, overview. In view of NADPH as the requisite reducing power in lipid production, the stability of malic enzyme is therefore crucial and malic enzyme activity is significant in the regulation of lipid accumulation
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metabolism
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the enzyme is involved in the fatty acid biosynthesis
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metabolism
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the enzyme is involved in the transhydrogenase cycle, overview. In view of NADPH as the requisite reducing power in lipid production, the stability of malic enzyme is therefore crucial and malic enzyme activity is significant in the regulation of lipid accumulation
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metabolism
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the enzyme is involved in the transhydrogenase cycle, overview. In view of NADPH as the requisite reducing power in lipid production, the stability of malic enzyme is therefore crucial and malic enzyme activity is significant in the regulation of lipid accumulation. The enzyme serves as the sole source of NADPH for fatty acid biosynthesis
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physiological function
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in those environments where glucose is very low or absent, the pathogen depends on NADP-linked dehydrogenases such as the MEs for NADPH production, as in those conditions the pentose phosphate pathway cannot serve as a source of essential reducing power
physiological function
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in those environments where glucose is very low or absent, the pathogen depends on NADP-linked dehydrogenases such as the MEs for NADPH production, as in those conditions the pentose phosphate pathway cannot serve as a source of essential reducing power
physiological function
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malate that is exported from the mitochondria to the cytosol is regenerated to pyruvate by cytosolic malic enzyme for cycling back to the mitochondria. Cytosolic malic enzyme, together with ATP citrate lyase and malate dehydrogenase, is also central to recycling of citrate back to pyruvate. Cytosolic malic enzyme in the beta-cell supports the concept that the mechanisms linking metabolism with insulin secretion may include a beta-cell pyruvate-malate cycle. siRNA knockdown and isotopic labeling strategies to evaluate the role of cytosolic and mitochondrial isozymes of malic enzyme in facilitating malate-pyruvate cycling in the context of fuel-stimulated insulin secretion, overview
physiological function
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NADP-ME in the C3 plants contributes to a huge diversity of metabolic pathways in green and non-green tissues of these plants. Additionally, NADP-ME increases its activity in the plant response to stresses
physiological function
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NADP-ME in the C3 plants contributes to a huge diversity of metabolic pathways in green and non-green tissues of these plants. Additionally, NADP-ME increases its activity in the plant response to stresses
physiological function
Mnium undulatum
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NADP-ME in the C3 plants contributes to a huge diversity of metabolic pathways in green and non-green tissues of these plants. Additionally, NADP-ME increases its activity in the plant response to stresses
physiological function
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NADP-ME in the C3 plants contributes to a huge diversity of metabolic pathways in green and non-green tissues of these plants. Additionally, NADP-ME increases its activity in the plant response to stresses
physiological function
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some pyruvate cycling pathways require malate export from mitochondria and NADP+-dependent decarboxylation of malate to pyruvate by cytosolic malic enzyme ME1. Role of ME1 in glucose-stimulated insulin secretion and in methyl succinate-stimulated insulin secretion occuring occur via succinate entry into the mitochondria in exchange for malate and subsequent malate conversion to pyruvate, overview
physiological function
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ADP-ME2 is an important player in plant basal defence, where it is involved in the generation of reactive oxygen species, NADP-ME2 is dispensable for later defence responses, overview
physiological function
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NADP-malic enzyme is the primary enzyme decarboxylating malate in bundle sheath cells to supply CO2 to Rubisco
physiological function
one isozyme exclusively expressed in the bundle sheath cells and involved in C4 photosynthesis, i.e. ZmC4-NADP-ME, and the other, ZmnonC4-NADP-ME, with housekeeping roles
physiological function
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possibly, in those environments where glucose is very low or absent, the pathogen depends on NADP-linked dehydrogenases such as the MEs for NADPH production, as in those conditions the pentose phosphate pathway cannot serve as a source of essential reducing power
physiological function
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possibly, in those environments where glucose is very low or absent, the pathogen depends on NADP-linked dehydrogenases such as the MEs for NADPH production, as in those conditions the pentose phosphate pathway cannot serve as a source of essential reducing power
physiological function
the enzyme plays a role in antibiotic and triacylglycerol production, e.g. production of the polyketide antibiotic actinorhodin, overview
physiological function
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enzyme activation in fruit exposed to 20% (v/v) CO2 provides NADPH for glutathione regeneration by glutathione reductase, thereby conferring protection against the cellular damage caused by low temperatures or excessive high CO2 levels
physiological function
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malic enzyme overexpression during the larval period lengthenes the lifespan of Drosophila melanogaster. Metabolic changes mediated by the enzyme during development are related to the control of reactive oxygen species tolerance and the longevity of Drosophila
physiological function
malic enzyme (ME) is a key enzyme regulating the lipid accumulation process in oleaginous microorganisms. It catalyzes the oxidative decarboxylation of L-malate to pyruvate and CO2 with concomitant reduction of NADP+ to NADPH, supplying the reducing power for fatty acid biosynthesis. The extent of lipid accumulation in some fungi is identified to be controlled by ME acting as the sole source of NADPH. Unique role of malic enzyme to provide NADPH for fatty acid synthesis as well as fatty acid desaturation
physiological function
malic enzyme (ME) is a key enzyme regulating the lipid accumulation process in oleaginous microorganisms. It catalyzes the oxidative decarboxylation of L-malate to pyruvate and CO2 with concomitant reduction of NADP+ to NADPH, supplying the reducing power for fatty acid biosynthesis. The extent of lipid accumulation in some fungi is identified to be controlled by ME acting as the sole source of NADPH. Unique role of malic enzyme to provide NADPH for fatty acid synthesis as well as fatty acid desaturation
physiological function
malic enzyme (ME) is a key enzyme regulating the lipid accumulation process in oleaginous microorganisms. It catalyzes the oxidative decarboxylation of L-malate to pyruvate and CO2 with concomitant reduction of NADP+ to NADPH, supplying the reducing power for fatty acid biosynthesis. The extent of lipid accumulation in some fungi is identified to be controlled by ME acting as the sole source of NADPH. Unique role of malic enzyme to provide NADPH for fatty acid synthesis as well as fatty acid desaturation
physiological function
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malic enzyme (ME) is a key enzyme regulating the lipid accumulation process in oleaginous microorganisms. It catalyzes the oxidative decarboxylation of L-malate to pyruvate and CO2 with concomitant reduction of NADP+ to NADPH, supplying the reducing power for fatty acid biosynthesis. The extent of lipid accumulation in some fungi is identified to be controlled by ME acting as the sole source of NADPH. Unique role of malic enzyme to provide NADPH for fatty acid synthesis as well as fatty acid desaturation. Activity of isoform E is intensely associated with the profiles and the level of lipid biosynthesis in N-limitation condition, while isoform D is reduced as lipid is produced. With ammonium tartrate as nitrogen source, activity of isoform D is pronounced, while isoform E is very low. Isoform E is the crucial regulator of lipid accumulation in strain 2A1
physiological function
malic enzyme (ME) is a key enzyme regulating the lipid accumulation process in oleaginous microorganisms. It catalyzes the oxidative decarboxylation of L-malate to pyruvate and CO2 with concomitant reduction of NADP+ to NADPH, supplying the reducing power for fatty acid biosynthesis. The extent of lipid accumulation in some fungi is identified to be controlled by ME acting as the sole source of NADPH. Unique role of malic enzyme to provide NADPH for fatty acid synthesis as well as fatty acid desaturation. The final governance over the malic enzyme activity is supposed to be the supply of its substrate
physiological function
mitochondrial NADP malic enzyme is necessary for insulin release
physiological function
NADP+-malic enzyme may not be the sole rate-limiting enzyme, but does play a role, during fatty acid synthesis in oleaginous fungi
physiological function
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pivotal role of malic enzyme in enhancing oil accumulation in green microalga Chlorella pyrenoidosa. The enzyme promte fatty acid biosynthesis
physiological function
significance of malic enzyme in fat synthesis. Malic enzyme is the main NADPH source in normoxic 3T3-L1 adipocytes, with total NADPH production more than double that from the oxidative pentose phosphate pathway
physiological function
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enzyme overexpression can simultaneously improve the carbon concentration and reducing power in cells, thereby increasing the lipid and fatty acid methyl ester yields of Nannochloropsis salina
physiological function
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enzyme overexpression in cancer cells leads to decreased cellular differentiation, enhanced invasiveness associated with cellular differentiation proteins, modulation of AKT and AMPK signalling, modulation of p53 levels and its downstream target p21, increased cellular growth rate and proliferation with decreasing apoptotic rate, as well as modulation of glutamine oxidation via the Krebs cycle
physiological function
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enzyme overexpression of Sorghum bicolor NADP-ME in Arabidopsis thaliana increases salt tolerance and alleviates photosystem II and photosystem I photoinhibition under salt stress by improving photosynthetic capacity
physiological function
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isoform ME1 contributes to increased internal malate and citrate concentrations and their external efflux to confer higher aluminium resistance
physiological function
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isoform NADP-ME1 activity is required for protecting seeds against oxidation during seed dry storage
physiological function
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isoform NADP-ME1 plays a specialized role, linked to abscisic acid signalling during the seed development as well as in the response to water deficit stress
physiological function
the enzyme is associated with resistance against the root-knot nematode Meloidogyne javanica in field pea
physiological function
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the enzyme is important for survival of Leishmania amastigotes within host macrophages
physiological function
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the enzyme plays an important role in maintaining the supply of NADPH during pepper fruit ripening
physiological function
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the enzyme plays important roles in diverse stress responses (pathogen infection, ozone stress, drought stress, salt stress, metal excess, temperature stress, wounding and UV radiation)
physiological function
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NADP+-malic enzyme may not be the sole rate-limiting enzyme, but does play a role, during fatty acid synthesis in oleaginous fungi
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physiological function
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in those environments where glucose is very low or absent, the pathogen depends on NADP-linked dehydrogenases such as the MEs for NADPH production, as in those conditions the pentose phosphate pathway cannot serve as a source of essential reducing power
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physiological function
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possibly, in those environments where glucose is very low or absent, the pathogen depends on NADP-linked dehydrogenases such as the MEs for NADPH production, as in those conditions the pentose phosphate pathway cannot serve as a source of essential reducing power
-
physiological function
-
malic enzyme (ME) is a key enzyme regulating the lipid accumulation process in oleaginous microorganisms. It catalyzes the oxidative decarboxylation of L-malate to pyruvate and CO2 with concomitant reduction of NADP+ to NADPH, supplying the reducing power for fatty acid biosynthesis. The extent of lipid accumulation in some fungi is identified to be controlled by ME acting as the sole source of NADPH. Unique role of malic enzyme to provide NADPH for fatty acid synthesis as well as fatty acid desaturation. Activity of isoform E is intensely associated with the profiles and the level of lipid biosynthesis in N-limitation condition, while isoform D is reduced as lipid is produced. With ammonium tartrate as nitrogen source, activity of isoform D is pronounced, while isoform E is very low. Isoform E is the crucial regulator of lipid accumulation in strain 2A1
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physiological function
-
malic enzyme (ME) is a key enzyme regulating the lipid accumulation process in oleaginous microorganisms. It catalyzes the oxidative decarboxylation of L-malate to pyruvate and CO2 with concomitant reduction of NADP+ to NADPH, supplying the reducing power for fatty acid biosynthesis. The extent of lipid accumulation in some fungi is identified to be controlled by ME acting as the sole source of NADPH. Unique role of malic enzyme to provide NADPH for fatty acid synthesis as well as fatty acid desaturation
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physiological function
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in those environments where glucose is very low or absent, the pathogen depends on NADP-linked dehydrogenases such as the MEs for NADPH production, as in those conditions the pentose phosphate pathway cannot serve as a source of essential reducing power
-
physiological function
-
possibly, in those environments where glucose is very low or absent, the pathogen depends on NADP-linked dehydrogenases such as the MEs for NADPH production, as in those conditions the pentose phosphate pathway cannot serve as a source of essential reducing power
-
physiological function
-
in those environments where glucose is very low or absent, the pathogen depends on NADP-linked dehydrogenases such as the MEs for NADPH production, as in those conditions the pentose phosphate pathway cannot serve as a source of essential reducing power
-
physiological function
-
possibly, in those environments where glucose is very low or absent, the pathogen depends on NADP-linked dehydrogenases such as the MEs for NADPH production, as in those conditions the pentose phosphate pathway cannot serve as a source of essential reducing power
-
physiological function
-
malic enzyme (ME) is a key enzyme regulating the lipid accumulation process in oleaginous microorganisms. It catalyzes the oxidative decarboxylation of L-malate to pyruvate and CO2 with concomitant reduction of NADP+ to NADPH, supplying the reducing power for fatty acid biosynthesis. The extent of lipid accumulation in some fungi is identified to be controlled by ME acting as the sole source of NADPH. Unique role of malic enzyme to provide NADPH for fatty acid synthesis as well as fatty acid desaturation. The final governance over the malic enzyme activity is supposed to be the supply of its substrate
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physiological function
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the enzyme plays a role in antibiotic and triacylglycerol production, e.g. production of the polyketide antibiotic actinorhodin, overview
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additional information
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analysis of transcriptional co-response patterns related NADP-ME2 to plant defence responses, overview
additional information
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reversal of ZmC4-NADP-ME oxidation by chemical reductants, e.g. iodosobenzoate and CuCl2, doe to the presence of thiol groups able to form disulfide bonds. Residues Cys192, Cys246, Cys270, and Cys410 may be directly or indirectly implicated in ZmC4-NADP-ME redox modulation. Redox regulation plays a key role in many plastid functions. Isozyme specific redox regulation of ZmC4-NADP-ME activity, the modulation is not observed in the case of isozyme ZmnonC4-NADP-ME. The replacement of Cys246 with serine in ZmnonC4-NADP-ME may be responsible for the absence of redox modulation
additional information
reversal of ZmC4-NADP-ME oxidation by chemical reductants, e.g. iodosobenzoate and CuCl2, doe to the presence of thiol groups able to form disulfide bonds. Residues Cys192, Cys246, Cys270, and Cys410 may be directly or indirectly implicated in ZmC4-NADP-ME redox modulation. Redox regulation plays a key role in many plastid functions. Isozyme specific redox regulation of ZmC4-NADP-ME activity, the modulation is not observed in the case of isozyme ZmnonC4-NADP-ME. The replacement of Cys246 with serine in ZmnonC4-NADP-ME may be responsible for the absence of redox modulation
additional information
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fatty acid composition analysis of wild-type and mutant overexpressing strains, overview
additional information
the molecular basis for the different allosteric properties and quaternary structural stability of m-NAD(P)-ME, EC 1.1.1.39 and c-NADP-ME, EC 1.1.1.40. The structural features near the fumarate binding site and the dimer interface are highly related to the quaternary structural stability of c-NADP-ME and m-NAD(P)-ME
additional information
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the molecular basis for the different allosteric properties and quaternary structural stability of m-NAD(P)-ME, EC 1.1.1.39 and c-NADP-ME, EC 1.1.1.40. The structural features near the fumarate binding site and the dimer interface are highly related to the quaternary structural stability of c-NADP-ME and m-NAD(P)-ME
additional information
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tracing carbon flux through malic enzyme, overview
additional information
tracing carbon flux through malic enzyme, overview