Glyceraldehyde 3-phosphate

Glyceraldehyde 3-phosphate bacterial metabolite produced during a metabolic reaction in Escherichia coli. Any mammalian metabolite produced during a metabolic reaction in humans Homo sapiens. Any eukaryotic metabolite produced during a metabolic reaction in plants, the kingdom that include flowering plants, conifers and other gymnosperms, glyceraldehyde 3-phosphate. Read more

D-glyceraldehyde 3-phosphate is formed from the following three compounds in reversible reactions:. Enzyme 4. The numbering of the carbon atoms indicates the fate of the carbons according to their position in fructose 6-phosphate. Enzyme 5. Enzyme 1.

Glyceraldehyde 3-phosphate

Glyceraldehydephosphate dehydrogenase GAPDH is a highly conserved enzyme within the glycolytic pathway. Two copies of genes encoding GAPDH were characterized, then endogenously overexpressed and silenced through Agrobacterium tumefaciens -mediated transformation methods. Analysis of metabolite and enzyme expression levels revealed that the increased lipid content of MA-GAPDH1 was due to enhanced flux of glyceraldehydephosphate to glycerate-1, 3-biphosphate. Mortierella alpina is an oleaginous filamentous fungus with a strong ability to accumulate polyunsaturated fatty acids PUFAs and has been used in industrial production of arachidonic acids ARA Tsunehiro et al. Great efforts have been made to improve its lipid yield, production and productivity Koike et al. A traditional and effective way to achieve this is increasing the supply of NADPH, which is indispensable during lipid biosynthesis. Known enzymes involved in this process include malic enzyme, glucosephosphate dehydrogenase and 6-phosphogluconic dehydrogenase from the phosphate pentose pathway and isocitrate dehydrogenase Hao et al. A clear understanding of all NADPH sources for lipid biosynthesis is important for expounding the lipid biosynthesis process. Studies aimed to identify enzymes that contribute to NADPH production for lipid biosynthesis are necessary. It catalyzes the conversion of glyceraldehyde 3-phosphate to glycerate-1, 3-biphosphate, and results in production of NADH. The gapdh is traditionally used as a conserved gene for species identification Ghuffar et al. Its promoter is highly effective for heterologous protein expression in microorganisms Madhavan et al.

Metabolic analysis of the pathways the overexpression transformants and RNA interference transformants A substrate and product analysis of the GAPDH pathway; B transcription level of the selected genes, glyceraldehyde 3-phosphate.

Federal government websites often end in. The site is secure. Glyceraldehydephosphate dehydrogenase GAPDH is a glycolytic enzyme whose role in cell metabolism and homeostasis is well defined, while its function in pathologic processes needs further elucidation. These interprotein interactions and post-translational modifications of GAPDH mediate its cytotoxic or cytoprotective functions in the manner of a Janus-like molecule. In this review, we discuss the functional features of the enzyme in cellular physiology and its possible involvement in human pathologies.

Federal government websites often end in. The site is secure. Supplementary Figures. DOI: The crystal structure of full-length glyceraldehydephosphate dehydrogenase type 1 GAPDH1 from Escherichia coli was determined at 1. Glyceraldehydephosphate dehydrogenase GAPDH is a key enzyme in the glycolytic pathway that catalyzes the conversion of d -glyceraldehyde 3-phosphate to 1,3-diphosphoglycerate. The protein has a certain amount of thermostability. The confirmed recombinant vectors were transformed into E.

Glyceraldehyde 3-phosphate

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Plant Dis. Glyceraldehydephosphate dehydrogenase. Colon carcinoma, cervical carcinoma. Chiche J. Last Modified. Hara M. Figure 4. National Center for Biotechnology Information, U. Oxidation of C causes an inactivation of GAPDH and the formation of intra- or inter-molecular disulfide bonds [ 64 , 65 ]. Finally, the data obtained on human aortic smooth muscle cells shows that the down-regulation of GAPDH glycolytic activity and subsequent ATP depletion caused alterations in arterial wall energy homeostasis leading to atherosclerotic pathogenesis [ 85 ].

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Mikhaylova E. Moreover, the cellular localization of GAPDH is not limited to the cytoplasm, the protein is found in the nucleus and other intracellular organelles [ 9 ], including plasma membrane [ 10 ]. According to the recent data, the PTP opening may be caused by the denatured GAPDH as a result of S-nitrosylation of C residue; the replacement of C with alanine resulted in the blockage of cell death in response to nitrosative stress [ 59 ], which proves the importance of GAPDH nitrosylation in regard to the advancement of apoptosis. Hyperglycemia, which remains an important factor in post-diabetes retinopathy, leads to a significant increase of nitrosylated GAPDH in retinal cells, which causes the intranuclear translocation of the enzyme and induction of apoptosis [ 33 , 61 ]. Any bacterial metabolite produced during a metabolic reaction in Escherichia coli. Up-regulation of glyceraldehydephosphate dehydrogenase gene expression by HIF-1 activity depending on Sp1 in hypoxic breast cancer cells. Homologous overexpression and RNA interference technology were used. Formation of exogenous cytotoxic aggregates. Samson A. Enzyme 5. Millet P. Data Br. Properties of substances inhibiting aggregation of oxidized GAPDH: Data on the interaction with the enzyme and the impact on its intracellular content. Fructose 6-phosphate.