5.4.2.12: phosphoglycerate mutase (2,3-diphosphoglycerate-independent)
This is an abbreviated version!
For detailed information about phosphoglycerate mutase (2,3-diphosphoglycerate-independent), go to the full flat file.
Word Map on EC 5.4.2.12
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5.4.2.12
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mutases
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2-phosphoglycerate
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ipgms
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2,3-bisphosphoglycerate-independent
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cofactor-dependent
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2,3-bisphosphoglycerate
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mexicana
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brugia
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malayi
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phosphoenzyme
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dikinase
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flux-controlling
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filariasis
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medicine
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drug development
- 5.4.2.12
- mutases
- 2-phosphoglycerate
-
ipgms
-
2,3-bisphosphoglycerate-independent
-
cofactor-dependent
- 2,3-bisphosphoglycerate
- mexicana
-
brugia
- malayi
- phosphoenzyme
- dikinase
-
flux-controlling
- filariasis
- medicine
- drug development
Reaction
Synonyms
2,3-biphosphoglycerate-independent phosphoglycerate mutase, 2,3-diphosphoglycerate-independent phosphoglycerate mutase, 2,3BPG-independent PGAM, 3-phosphoglycerate mutase, apgM, co-factor-independent phosphoglycerate mutase, cofactor independent phosphoglycerate mutase, cofactor-independent phosphoglycerate mutase, cofactor-independent phosphoglycerate mutase 1, EC 2.7.5.3, EC 5.4.2.1, independent PGAM, independent PGM, iPGAM, iPGM, MJ0010, MJ1612, PGAM, PGM, PH0037, SSO0417
ECTree
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General Information on EC 5.4.2.12 - phosphoglycerate mutase (2,3-diphosphoglycerate-independent)
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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
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
physiological function
additional information
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
physiological function
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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
additional information
ligand-induced conformational changes, overview
