EC Number   |
General Information |
Reference |
|---|
    5.4.2.12 | evolution |
PGAMs that are dependent on (EC 5.4.2.11) or independent of the 2,3-bisphosphoglycerate cofactor are members of two distinct protein families |
727472 |
| 5.4.2.12 | malfunction |
PMG1/PMG2 double mutants have no detectable iPGAM activity and show defects in blue light-, abscisic acid-, and low CO2-regulated stomatal movements. Vegetative plant growth is severely impaired in the double mutants and pollen is not produced, phenotypes, overview |
728053 |
| 5.4.2.12 | more |
ligand-induced conformational changes, overview |
727472 |
| 5.4.2.12 | physiological function |
2,3-biphosphoglycerate-independent phosphoglycerate mutase is a key enzymatic activity in glycolysis and catalyses the reversible interconversion of 3-phosphoglycerate to 2-phosphoglycerate, functions of iPGAMs and glycolysis in stomatal function and plant growth, overview. Both isozymes PMG1 and PMG2 and glycolytic activity are critical for guard cell function and fertility |
728053 |
| 5.4.2.12 | physiological function |
the enzyme modulates macrophage signaling and promotes T-cell repertoires bearing epitopes for both major histocompatibility complex classes I and II. Enzyme stimulation induces higher expression of interleukin (IL)-1beta in the phagocytic cell, its receptor and CD69 on T-cell subsets. These cellular activations result in upregulation of host-protective cytokines IL-2, IL-12, IL-17, tumour necrosis factor-alpha and interferon-gamma and downregulation of IL-4, IL-10 and tumour growth factor-beta. Enzyme stimulation also promotes lymphocyte proliferation and boosted the leishmaniacidal activity of macrophages by upregulating reactive oxygen species. It also induces 1.8fold higher release of nitric oxide by promoting the transcription of inducible nitric oxide synthase gene |
748833 |
