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
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Systematic Name
Systematic Name on EC 5.4.2.12 - phosphoglycerate mutase (2,3-diphosphoglycerate-independent)
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D-phosphoglycerate 2,3-phosphomutase (2,3-diphosphoglycerate-independent)
The enzymes from higher plants, algae, some fungi, nematodes, sponges, coelenterates, myriapods, arachnids, echinoderms, archaea and some bacteria (particularly Gram-positive) have maximum activity in the absence of 2,3-bisphospho-D-glycerate. cf. EC 5.4.2.11 phosphoglycerate mutase (2,3-diphosphoglycerate-dependent). The enzyme contains two Mn2+ (or in some species two Co2+ ions). The reaction involves a phosphotransferase reaction to serine followed by transfer back to the glycerate at the other position. Both metal ions are involved in the reaction.