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malfunction
dme mutants of the broad-host-range Sinorhizobium sp. strain NGR234 form nodules whose level of N2 fixation vary from 27 to 83% (plant dry weight) of the wild-type level, depending on the host plant inoculated. The single dme mutant fixes N2 at reduced rate. A pckA dme double mutant has no N2-fixing activity, PCK is phosphoenolpyruvate carboxykinase. Symbiotic phenotypes of NGR234 and NGR234 dme mutants on different host plants, overview
malfunction
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the single Sco2951 and the double Sco2951 Sco5261 mutants, deficient in ME-NAD and ME-NADP, EC 1.1.1.40, activity, display a strong reduction in the production of the polyketide antibiotic actinorhodin. Additionally, the Sco2951/Sco5261 mutant shows a decrease in stored triacylglycerides during exponential growth
malfunction
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knockdown of ME1 does not inhibit insulin release stimulated by glucose, pyruvate or 2-aminobicyclo [2,2,1]heptane-2-carboxylic acid-plus-glutamine
malfunction
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the single Sco2951 and the double Sco2951 Sco5261 mutants, deficient in ME-NAD and ME-NADP, EC 1.1.1.40, activity, display a strong reduction in the production of the polyketide antibiotic actinorhodin. Additionally, the Sco2951/Sco5261 mutant shows a decrease in stored triacylglycerides during exponential growth
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malfunction
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dme mutants of the broad-host-range Sinorhizobium sp. strain NGR234 form nodules whose level of N2 fixation vary from 27 to 83% (plant dry weight) of the wild-type level, depending on the host plant inoculated. The single dme mutant fixes N2 at reduced rate. A pckA dme double mutant has no N2-fixing activity, PCK is phosphoenolpyruvate carboxykinase. Symbiotic phenotypes of NGR234 and NGR234 dme mutants on different host plants, overview
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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
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the malic enzyme is involved in the (S)-malate catabolic pathways and the putative gluconeogenic pathways, overview
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
Lacticaseibacillus casei BL23 and ATCC 334
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the malic enzyme is involved in the (S)-malate catabolic pathways and the putative gluconeogenic pathways, overview
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physiological function
for a metabolic condition in which the mitochondrial NAD level is low and the (S)-malate level is high, the activity of homodimeric isozyme NAD-ME2 and/or heterodimer NAD-MEH would be preferred over that of homodimeric isozyme NAD-ME1
physiological function
malic enzyme plays an important role in the metabolic regulation under photoheterotrophic conditions, carbon metabolic pathway, overview
physiological function
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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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the malic enzyme pathway enables Lactobacillus casei to grow on L-malic acid., requirement of the MaeKR two-component system for L-malic acid utilization via a malic enzyme pathway, overview
physiological function
AZC3656 protein is a NAD+-malic enzyme, i.e. DME, while AZC0119 protein is not a malic enzyme. DME is considered an important enzyme for regulating C4-dicarboxylic acid metabolism in N2-fixing bacteroids because its activity is strongly inhibited by acetyl-CoA and stimulated by fumarate and succinate. The NAD+-malic enzyme is required for N2 fixation, and this activity is thought to be required for the anaplerotic synthesis of pyruvate. But NGR234 bacteroids appear to synthesize pyruvate from TCA cycle intermediates via DME or PCK, phosphoenolpyruvate carboxykinase, pathways, overview
physiological function
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DME is considered an important enzyme for regulating C4-dicarboxylic acid metabolism in N2-fixing bacteroids because its activity is strongly inhibited by acetyl-CoA and stimulated by fumarate and succinate. The NAD+-malic enzyme is required for N2 fixation, and this activity is thought to be required for the anaplerotic synthesis of pyruvate
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
physiological function
plant mitochondria can use L-malate and fumarate, which accumulate in large levels, as respiratory substrates. In part, this property is due to the presence of NAD-dependent malic enzymes (NAD-ME). Malic enzyme tracers reveal hypoxia-induced switch in adipocyte NADPH pathway usage
physiological function
Plant mitochondria can use L-malate and fumarate, which accumulate in large levels, as respiratory substrates. In part, this property is due to the presence of NAD-dependent malic enzymes (NAD-ME). Malic enzyme tracers reveal hypoxia-induced switch in adipocyte NADPH pathway usage. Important role of NAD-ME1 in processes that control flow of C4 organic acids in Arabidopsis mitochondrial metabolism.. NAD-ME1 exhibits a complex homo and heterotrophic allosteric regulation with L-malate wielding an inhibitory effect that is cancelled by competitive fumarate binding
physiological function
Lacticaseibacillus casei BL23 and ATCC 334
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the malic enzyme pathway enables Lactobacillus casei to grow on L-malic acid., requirement of the MaeKR two-component system for L-malic acid utilization via a malic enzyme pathway, overview
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physiological function
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malic enzyme plays an important role in the metabolic regulation under photoheterotrophic conditions, carbon metabolic pathway, overview
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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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physiological function
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AZC3656 protein is a NAD+-malic enzyme, i.e. DME, while AZC0119 protein is not a malic enzyme. DME is considered an important enzyme for regulating C4-dicarboxylic acid metabolism in N2-fixing bacteroids because its activity is strongly inhibited by acetyl-CoA and stimulated by fumarate and succinate. The NAD+-malic enzyme is required for N2 fixation, and this activity is thought to be required for the anaplerotic synthesis of pyruvate. But NGR234 bacteroids appear to synthesize pyruvate from TCA cycle intermediates via DME or PCK, phosphoenolpyruvate carboxykinase, pathways, overview
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additional information
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deletion of either the gene encoding the histidine kinase or the response regulator of the TC system results in the loss of the ability to grow on L-malic acid, thus indicating that the cognate TC system regulates and is essential for the expression of malic enzyme. Expression of maeE is induced in the presence of L-malic acid and repressed by glucose, whereas TC system expression is induced by L-malic acid and is not repressed by glucose
additional information
enzyme activity is allosterically regulated by acetyl-CoA
additional information
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higher expression of ME2 correlates with the degree of cell de-differentiation. Knockdown of ME2 leads to induction of erythroid differentiation, and diminished proliferation of tumor cells and increased apoptosis in vitro. ME2 knockdown also totally abolishes growth of K562 cells in nude mice. Depletion of endogenous ME2 levels enhances reactive oxygen species, increases NAD+/NADH and NADP+/NADPH ratio and inhibits ATP production in K562 cells. ME2 depletion resulted in high orotate levels, suggesting potential impairment of pyrimidine metabolism
additional information
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identification of specific domains of the primary structure, which are involved in the differential allosteric regulation. Different properties of NAD-ME1, -2, and -H, mitochondrial NAD-ME activity may be regulated by varying native association in vivo, rendering enzymatic entities with distinct allosteric regulation to fulfill specific roles, overview
additional information
identification of specific domains of the primary structure, which are involved in the differential allosteric regulation. Different properties of NAD-ME1, -2, and -H, mitochondrial NAD-ME activity may be regulated by varying native association in vivo, rendering enzymatic entities with distinct allosteric regulation to fulfill specific roles, overview
additional information
identification of specific domains of the primary structure, which are involved in the differential allosteric regulation. Different properties of NAD-ME1, -2, and -H, mitochondrial NAD-ME activity may be regulated by varying native association in vivo, rendering enzymatic entities with distinct allosteric regulation to fulfill specific roles, overview
additional information
interaction between NAD-ME1 and -ME2 generates a heteromeric enzyme NAD-MEH with a particular kinetic behaviour. The N-terminal region of NAD-ME1 and -ME2 is associated with the order of substrate binding. The chimeric enzyme NAD-ME1q, that is composed of the first 176 amino acid residues of NAD-ME2 and the central and C-terminal sequence of NAD-ME1, shows a hyperbolic behaviour for (S)-malate and NAD+. Product-inhibition pattern of NAD-ME1q with the three products supports a sequential ordered mechanism
additional information
interaction between NAD-ME1 and -ME2 generates a heteromeric enzyme NAD-MEH with a particular kinetic behaviour. The N-terminal region of NAD-ME1 and -ME2 is associated with the order of substrate binding. The chimeric enzyme NAD-ME1q, that is composed of the first 176 amino acid residues of NAD-ME2 and the central and C-terminal sequence of NAD-ME1, shows a hyperbolic behaviour for (S)-malate and NAD+. Product-inhibition pattern of NAD-ME1q with the three products supports a sequential ordered mechanism
additional information
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interaction between NAD-ME1 and -ME2 generates a heteromeric enzyme NAD-MEH with a particular kinetic behaviour. The N-terminal region of NAD-ME1 and -ME2 is associated with the order of substrate binding. The chimeric enzyme NAD-ME1q, that is composed of the first 176 amino acid residues of NAD-ME2 and the central and C-terminal sequence of NAD-ME1, shows a hyperbolic behaviour for (S)-malate and NAD+. Product-inhibition pattern of NAD-ME1q with the three products supports a sequential ordered mechanism
additional information
mutants and chimeric proteins of NAD-ME1 and -2 indicated that the amino-terminal region of NAD-ME1 is implicated in fumarate activation and sigmoidal L-malate responses, structure-function analysis, overview
additional information
mutants and chimeric proteins of NAD-ME1 and -2 indicated that the amino-terminal region of NAD-ME1 is implicated in fumarate activation and sigmoidal L-malate responses, structure-function analysis, overview
additional information
residues Arg50, Arg80 and Arg84 show different roles in organic acid binding. These residues form a triad, which is the basis of the homo and heterotrophic effects that characterize NAD-ME1. Mutants and chimeric proteins of NAD-ME1 and -2 indicated that the amino-terminal region of NAD-ME1 is implicated in fumarate activation and sigmoidal L-malate responses, structure-function analysis, overview
additional information
residues Arg50, Arg80 and Arg84 show different roles in organic acid binding. These residues form a triad, which is the basis of the homo and heterotrophic effects that characterize NAD-ME1. Mutants and chimeric proteins of NAD-ME1 and -2 indicated that the amino-terminal region of NAD-ME1 is implicated in fumarate activation and sigmoidal L-malate responses, structure-function analysis, overview
additional information
Lacticaseibacillus casei BL23 and ATCC 334
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deletion of either the gene encoding the histidine kinase or the response regulator of the TC system results in the loss of the ability to grow on L-malic acid, thus indicating that the cognate TC system regulates and is essential for the expression of malic enzyme. Expression of maeE is induced in the presence of L-malic acid and repressed by glucose, whereas TC system expression is induced by L-malic acid and is not repressed by glucose
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additional information
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enzyme activity is allosterically regulated by acetyl-CoA
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