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
-
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
- 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
Advanced search results
Metals Ions
Metals Ions on EC 5.4.2.12 - phosphoglycerate mutase (2,3-diphosphoglycerate-independent)
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Co2+
CoCl2
inhibition by EDTA is reversible by incubation with CoCl2, but not MnCl2, FeSO4, CuSo4, NiCl2, ZnCl2
Mg2+
Mn2+
additional information
-
required for activity, 2fold higher activity at 0.4 mM than with 0.5 mM Mn2+
Co2+
divalent cation required for activity, 3times higher activity than with Mn2+
Co2+
two metal sites (M1 and M2) containing cobalt ions are present in the phosphatase domain of the enzyme structure, interaction between Asp319 and the metal bound to the active site, contribution to the domain movement
-
in presence of 5 mM Mg2+, 2-3fold stimulation by 0.05 mM Mn2+. Mn2+ and Mg2+ are required for thermal stability
Mn2+
absolutely required for activity, maximal activation at 1 mM
Mn2+
-
activation, best achieved in buffer of tetramethylenediamine tetraacetate or trimethylenediamine tetraacetate
Mn2+
-
specific activator, none of the metal ions tested reaches more than 4% of the activity of EDTA-treated enzyme reactivated with Mn2+. Activation by Mn2+ is strongly pH-dependent within the physiological range
additional information
-
Cd2+, Zn2+, Fe2+, Ni2+, Cu2+, Mg2+, Ca2+, Sr2+, or Ba2+ give no more than 4% of the activity of EDTA-treated enzyme reactivated with Mn2+