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Malate can be oxidized to oxaloacetate by removal of two hydrogen atoms, which are accepted by NAD+.
Catalyzed by ME, malate can be converted into pyruvate, accompanied by NADPH.
Malate can be utilized (with very low biomass yields) under these conditions by employing the fumarate reductase as a mechanism for ATP generation.
Malate can be metabolized through other pathway (TCA cycle, GOC cycle, and so on) and thus reduce carbon loss through the photorespiratory pathway.
In plants, malate can be decarboxylated in the mitochondrial matrix through the action of NAD-ME to produce pyruvate, which is oxidized by the tricarboxylic acid cycle.
In the cytoplasm, malate can be produced from PEP produced in glycolysis through the activities of phosphoenolpyruvate carboxylase (PEPC) and malate dehydrogenase.
Similar(53)
This is in line with our experiments on minimal medium for L. hongkongensis which showed that L-malate can be used as sole carbon source [ 11].
The presence of high number of C4-dicarboxylates transporters may reflect the ability of using C4-dicarboxylates as carbon sources in L. hongkongensis, as the bacterium is assacharolytic, lacking a complete glycolytic pathway, and is in line with our experiments showing that L-malate can be used as its sole carbon source [ 14].
Specifically, HtrA in combination with malate synthase can be used in GSMN-TB to generate biomass and NGAM.
This metabolic program is thought to potentiate the evolution of Cit+ by increasing the production of C4-dicarboxylates (succinate, fumarate, and malate) which can be exported in exchange for citrate uptake by the CitT antiporter.
Similarly, the gene for malate dehydrogenase was not found, but oxidation of malate into oxaloacetate can be catalyzed by malate:quinone oxidoreductase (mqo; APA386B_2675; Figure 4, reaction 48) [ 59].
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