EC Number   |
General Information |
Reference |
|---|
    2.7.9.1 | drug target |
the pyruvate phosphate dikinase inhibitor Z220582104 is significantly leishmanicidal against the promastigotes and intracellular amastigotes. The study of pyruvate phosphate dikinase in parasitic organisms is significant because the enzyme is absent in the mammalian host which has different catalytic mechanisms for the glycolytic pathway |
-, 761254 |
| 2.7.9.1 | evolution |
three-dimensional modeling of PPDKs from divergent organisms and comparion of the orientation of the phosphorylatable histidine residue within the central domain of PPDKs. These PPDKs are compared using a maximum-likelihood tree. For PPDK from anaerobic protozoans, the central domain tilt toward the N-terminal nucleotide-binding domain, indicating that this enzyme catalyzes ATP synthesis, phylogenetic analysis of the N- and C-terminal sequences of PPDKs from different species, overview. PPDK in anaerobic organisms is functionally adapted to generate energy more efficiently in an anaerobic environment |
738071 |
| 2.7.9.1 | evolution |
three-dimensional modeling of PPDKs from divergent organisms and comparion of the orientation of the phosphorylatable histidine residue within the central domain of PPDKs. These PPDKs are compared using a maximum-likelihood tree. For PPDK from Giardia, as well as from other anaerobic protozoans, the central domain tilt toward the N-terminal nucleotide-binding domain, indicating that this enzyme catalyzes ATP synthesis, phylogenetic analysis of the N- and C-terminal sequences of PPDKs from different species, overview. PPDK in anaerobic organisms, e.g. the enzyme from Giardia lamblia, is functionally adapted to generate energy more efficiently in an anaerobic environment |
738071 |
| 2.7.9.1 | evolution |
three-dimensional modeling of PPDKs from divergent organisms and comparion of the orientation of the phosphorylatable histidine residue within the central domain of PPDKs. These PPDKs are compared using a maximum-likelihood tree. Phylogenetic analysis of the N- and C-terminal sequences of PPDKs from different species, overview |
738071 |
| 2.7.9.1 | evolution |
Trypanosoma evansi does not undergo stage-dependent differentiations, it occurs only as bloodstream forms, the metabolic pattern of this parasite is not identical to that of the bloodstream form of Trypanosoma brucei, modelling, overview |
-, 738185 |
| 2.7.9.1 | malfunction |
a reduction in PPDK activities due to high temperature (31°C) is observed during the middle and late grain filling periods, accompanied by downregulated cyPPDK mRNA and protein levels, leading to high temperature-induced chalkiness. Rice chalkiness due to high temperature during grain filling lower the grain quality. Temperature effects on the developmental regulation of PPDK activity are confirmed at transcription, translation and post-translational levels. Comparison of rice grain types at 24°C and 31°C of the two cultivars, overview |
739337 |
| 2.7.9.1 | malfunction |
an opaque phenotype results complete pyruvate phosphate dikinase knockout, including loss of vitreous endosperm character |
762279 |
| 2.7.9.1 | malfunction |
Brucella suis 513 attenuation occurrs only in the double phosphoenolpyruvate carboxykinase (PckA) / pyruvate phosphate dikinase (PpdK) mutant |
-, 761159 |
| 2.7.9.1 | malfunction |
deletion of the trypanosomal PPDK gene affects glycolysis. The rate of acetate production from glucose is 30% reduced in the DELTAppdk mutant, whereas threonine-derived acetate production is not affected. The DELTAppdk/DELTApepck double mutant, also lacking phosphoenolpyruvate carboxykinase, PEPCK, is incubated in glucose as the only carbon source and shows a 3.8fold reduction of the glycolytic rate compared with the DELTApepck mutant, as a consequence of the imbalanced glycosomal ATP/ADP ratio. Expressing the glycosomal phosphoglycerate kinase (PGKC) in the DELTAppdk/DELTApepck cell line restores the glycolytic flux, but expression of PGKC is lethal for procyclic trypanosomes, as a consequence of ATP depletion, due to glycosomal relocation of cytosolic ATP production. Comparison of glucose metabolism regulation of wild-type and mutant enzymes, the glucose metabolism is strongly impaired in the DELTAppdk/DELTApepck mutant, overview |
-, 738616 |
| 2.7.9.1 | malfunction |
in gluconeogenic but not in rich media, growth of enzyme-deficient mutant DELTAppdK is severely impaired. In RAW 264.7 macrophages, the DELTAppdK mutant shows reduced multiplication, and studies with the DELTAppdK mutant confirm that it reaches the replicative niche. The mutant is attenuated in mice being cleared by week 10 |
-, 738533 |
