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evolution
the PGKB transcript is approximately three-fold more abundant than the PGKC transcript in promastigotes
evolution
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the PGKB transcript is approximately three-fold more abundant than the PGKC transcript in promastigotes
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malfunction
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targeted disruption of Pgk2 by homologous recombination eliminates PGK activity in sperm and testis, and severely impairs male fertility, but does not block spermatogenesis. Mating behavior, reproductive organ weights (testis, excurrent ducts, and seminal vesicles), testis histology, sperm counts, and sperm ultrastructure are indistinguishable between Pgk2(-/-) and wild-type mice. Sperm motility and ATP levels are markedly reduced in males lacking PGK2. Pgk2(-/-) males sire occasional pups. Alternative pathways that bypass the PGK step of glycolysis exist. One of these bypass enzymes, acylphosphatase, is active in mouse sperm, perhaps contributing to phenotypic differences between mice lacking GAPDHS or PGK2
malfunction
mutations in hPGK1 cause human PGK1 deficiency, a rate metabolic conformational disease. Most of these mutations cause protein kinetic destabilization by significant changes in the structure/energetics of the transition state for irreversible denaturation. Protein kinetic destabilization by acidic pH is strongly linked to lower thermodynamic stability, while in disease-causing mutations seems to be linked to lower unfolding cooperativity. The plasticity of the hPGK1 denaturation mechanism responds differently to changes in pH and in disease-causing mutations
malfunction
reduction of PGK decreases the accumulation of Bamboo mosaic virus BaMV coat protein
malfunction
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an enzyme-deficient mutant can grow in medium with glucose, galactose, fructose, mannose or sucrose, as the sole carbon source, cannot utilize pyruvate, and shows a reduction of extracellular polysaccharide biosynthesis, cell motility, and intracellular ATP. As a result, the virulence of the enzyme-deficient mutant is significantly compromised in host soybean
malfunction
perturbation of enzyme form PGK1 in cancer cells insignificantly affects the conversion of glucose to lactate in glycolysis. Enzyme knockdown does not significantly affect the glycolysis rate, moderately reduces serine consumption and de novo serine synthesis
malfunction
plants with single mutations in the plastidial enzyme gene pgkp1 are not significantly affected, whereas a pgkp1pgkp2 double mutation is lethal due to retarded carbon fixation. Mutants are albino due to a plastid-oriented galactoglycerolipid deficiency
malfunction
plants with single mutations in the plastidial enzyme gene pgkp2 are not significantly affected, whereas a pgkp1pgkp2 double mutation is lethal due to retarded carbon fixation. Mutants are albino due to a plastid-oriented galactoglycerolipid deficiency
malfunction
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an enzyme-deficient mutant can grow in medium with glucose, galactose, fructose, mannose or sucrose, as the sole carbon source, cannot utilize pyruvate, and shows a reduction of extracellular polysaccharide biosynthesis, cell motility, and intracellular ATP. As a result, the virulence of the enzyme-deficient mutant is significantly compromised in host soybean
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metabolism
PGK1 is a potentially light-modulated Calvin-Benson cycle enzyme
metabolism
anaerobic fermentative metabolism of glycerol. Proteome analysis as well as enzyme assays performed in cell-free extracts demonstrate that glycerol is degraded via glyceraldehyde-3-phosphate, which is further metabolized through the lower part of glycolysis leading to formation of mainly ethanol and hydrogen
metabolism
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cytosolic isoform Pgk3 is involved in glycolysis (ATP production) while isoforms Pgk1 and Pgk2 are specific for plastid photosynthesis (ATP consumption)
metabolism
the enzyme acts as a pro-viral host factor. Tomato bushy stunt virus co-opts the glycolytic ATP-generating phosphoglycerate kinase 1 to facilitate the intracellular assembly of new viral replicase complexes
metabolism
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the enzyme is involved in carbohydrate utilization, extracellular polysaccharide biosynthesis, and cell motility of Xanthomonas axonopodis pv. glycines independent of Crp-like protein
metabolism
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the enzyme is involved in carbohydrate utilization, extracellular polysaccharide biosynthesis, and cell motility of Xanthomonas axonopodis pv. glycines independent of Crp-like protein
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physiological function
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overexpression of PGK1 can restore normal ageing of cells and suppress other apoptotic phenotypes of the MCY4/313Kllsm4DELTA1 mutant strain, including chromatin fragmentation and sensitivity to acetic acid, H2O2 and caffeine
physiological function
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PGK1 helps support the interactions between cancer and its microenvironment. A direct and facilitating relationship between CXCL12 and PGK1 levels in the tumor stroma, overexpression of PGK1 increases expression of CXCL12 compared with controls, whereas reducing PGK1 expression decreases expression of CXCL12 levels by cancer-associated fibroblasts. Coimplantation of PGK1-overexpressing fibroblasts with prostate tumor cells promote tumor cell growth in vivo. PGK1 expression in normal fibroblasts stimulates PCalpha proliferation and invasion. Expression of PGK1 and CXCL12 by normal fibroblasts contributes to expression of cancer-associated fibroblast phenotype. Reduced CXCR4 levels in normal fibroblasts that overexpress PGK1
physiological function
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PGK1 regulates the expression of CXCR4 and beta-catenin at the mRNA and protein levels. PGK1 and CXCR4 regulate their expression reciprocally. Overexpression of PGK1 dramatically increases the invasiveness of gastric cancer cells. Inhibition of CXCR4 in cells overexpressing PGK1 produces only a moderate reduction of invasiveness suggesting that, PGK1 itself has a critical role in tumor invasiveness. PGK1 may be a crucial enzyme in peritoneal dissemination, enhanced expression of PGK1 and its signaling targets CXCR4 and beta-catenin in gastric cancer cells promote peritoneal carcinomatosis
physiological function
Pgk1/EGFP expression in ovaries is effective in protecting the fecundity of the partial ovaries after ovary allotransplantation
physiological function
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PGK2 is not required for completion of spermatogenesis, but is essential for sperm motility and male fertility
physiological function
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phosphoglycerate kinase-1 and histone H4 elicit a significant differential humoral response in cancer sera compared with age- and sex-matched sera from normal patients and patients with chronic pancreatitis and diabetes
physiological function
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Synechocystis phosphoglycerate kinase is inactivated by oxidation and the oxidized enzyme is easily reduced and reactivated by thioredoxin, suggesting a role for thioredoxin in the control of the redox state of this enzyme
physiological function
gluconeogenic pathway
physiological function
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the enzyme is involved in glycogen catabolism
physiological function
3-phosphoglycerate kinase catalyzes phosphoryl transfer from 1,3-biphosphoglycerate to ADP to yield 3-phosphoglycerate and ATP in substrate chain phosphorylation. The enzyme is essential for growth of the organism with carbon sources requiring glycolysis and gluconeogenesis, critical role of PGK in
physiological function
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3-phosphogycerate kinase is a two domain enzyme, which transfers a phosphate group between its two substrates, 1,3-bisphosphoglycerate bound to the N-domain and ADP bound to the C-domain
physiological function
human phosphoglycerate kinase 1 is a glycolytic enzyme essential for ATP synthesis, and it is implicated in different pathological conditions such as inherited diseases, oncogenesis and activation of drugs for cancer and viral treatments. Enzyme PGK catalyzes the reversible phosphotransfer from ATP to 3-phosphoglycerate yielding ADP and 1,3-biphosphoglycerate, an essential step for ATP synthesis in the glycolytic pathway
physiological function
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PGK is the enzyme responsible for the first ATP generating step of glycolysis, The enzyme implicated in oncogenesis and the in vivo activation of L-nucleoside pro-drugs effective against retroviruses. Its mechanism requires considerable hinge bending to bring the substrates into proximity in order for phosphoryl transfer to occur. PGK activity is used as a signalling mechanism in oncogenesis, where it displays activity as a disulphide reductase
physiological function
PGK1 is involved in spermatogenesis and is related to sperm motility
physiological function
PGK2 is involved in spermatogenesis and is related to sperm motility
physiological function
phosphoglycerate kinase is an ATP-generating enzyme that acts in the glycolytic, gluconeogenic, and photosynthetic pathways. Chloroplast phosphoglycerate kinase is involved in the targeting of Bamboo mosaic virus to chloroplasts in Nicotiana benthamiana plants, the BaMV replicative intermediate exists in chloroplasts
physiological function
phosphoglycerate kinase plays a major role for ATP production during glycolysis and 1, 3-bisphosphoglycerate production to participate in the Calvin cycle for carbon fixation in plants
physiological function
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the surface located enzyme functions as an antigen in the host tilapia, Oreochromis niloticus, infected by Streptococcus agalactiae. The enzyme subunit can be used as vaccine in tilapia, overview
physiological function
thioredoxin-dependent redox regulation of chloroplastic phosphoglycerate kinase via oxidoreduction of the Cys227-Cys361 disulfide bond. Based on molecular mechanics calculation, the formation of the disulfide is proposed to impose structural constraints in the C-terminal domain of the enzyme that may lower its catalytic efficiency
physiological function
phosphoglycerate kinase 1 phosphorylates Beclin1 at Ser30 to enhance phosphatidylinositol 3-kinase VPS34 activity and to induce autophagy which is instrumental for brain tumor development
physiological function
the enzyme is involved in spermatogenesis and related to sperm motility
physiological function
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gluconeogenic pathway
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physiological function
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3-phosphoglycerate kinase catalyzes phosphoryl transfer from 1,3-biphosphoglycerate to ADP to yield 3-phosphoglycerate and ATP in substrate chain phosphorylation. The enzyme is essential for growth of the organism with carbon sources requiring glycolysis and gluconeogenesis, critical role of PGK in
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physiological function
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the surface located enzyme functions as an antigen in the host tilapia, Oreochromis niloticus, infected by Streptococcus agalactiae. The enzyme subunit can be used as vaccine in tilapia, overview
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additional information
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Brownian forces acting on the protein are the dominant factor in the catalytic cycle, the enzyme has evolved measures to harness this force for efficient catalysis. PGK is composed of two domains with the 3-phospho-D-glycerate or 3-phospho-D-glyceroyl phosphate binding site in the N-domain and the nucleotide binding site in the C-domain. In the absence of substrates, the enzyme is in an open conformation in which the two sites are separated and exposed to the solvent for rapid substrate/product exchange. In order for catalysis to occur, hinge bending leads to a closed conformation that results the formation of the active site and the correct placement of the substrates for nucleophilic attack. Structure of open and closed enzyme conformation, modelling, overview
additional information
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indispensable for the phosphoryl transfer reaction is a large conformational change from an inactive open to an active closed conformation via a hinge motion that should bring substrates into close proximity, molecular dynamics simulations, network-like representation of significant changes in inter-atomic forces, hydrogen-bond network in hinge bending region of apo and complexed hPGK, overview
additional information
protein conformation, thermodynamic and kinetic stability in hPGK1, overview. pH-Dependent linkage between decreased thermal kinetic stability and thermodynamic stability. hPGK1 remains in a native conformation at pH 5-8, but undergoes a conformational transition to a molten globule-like state at acidic pH. hPGK1 kinetic stability remains essentially constant at pH 6-8, but is significantly reduced when pH is decreased from pH 6 to pH 5. This decrease in kinetic stability is caused by significant changes in the energetic/structural balance of the denaturation transition state, which diverge from those found for disease-causing mutations. Protein kinetic destabilization by acidic pH is strongly linked to lower thermodynamic stability, while in disease-causing mutations seems to be linked to lower unfolding cooperativity. The plasticity of the hPGK1 denaturation mechanism responds differently to changes in pH and in disease-causing mutations
additional information
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protein conformation, thermodynamic and kinetic stability in hPGK1, overview. pH-Dependent linkage between decreased thermal kinetic stability and thermodynamic stability. hPGK1 remains in a native conformation at pH 5-8, but undergoes a conformational transition to a molten globule-like state at acidic pH. hPGK1 kinetic stability remains essentially constant at pH 6-8, but is significantly reduced when pH is decreased from pH 6 to pH 5. This decrease in kinetic stability is caused by significant changes in the energetic/structural balance of the denaturation transition state, which diverge from those found for disease-causing mutations. Protein kinetic destabilization by acidic pH is strongly linked to lower thermodynamic stability, while in disease-causing mutations seems to be linked to lower unfolding cooperativity. The plasticity of the hPGK1 denaturation mechanism responds differently to changes in pH and in disease-causing mutations
additional information
three-dimensional enzyme structure modeling and molecular dynamics, overview
additional information
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three-dimensional enzyme structure modeling and molecular dynamics, overview