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Information on EC 5.4.2.11 - phosphoglycerate mutase (2,3-diphosphoglycerate-dependent) and Organism(s) Saccharomyces cerevisiae and UniProt Accession P00950

for references in articles please use BRENDA:EC5.4.2.11
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EC Tree
IUBMB Comments
The enzymes from vertebrates, platyhelminths, mollusks, annelids, crustaceans, insects, algae, some fungi and some bacteria (particularly Gram-negative) require 2,3-bisphospho-D-glycerate as a cofactor. The enzyme is activated by 2,3-bisphospho-D-glycerate by transferring a phosphate to histidine (His10 in man and Escherichia coli, His8 in Saccharomyces cerevisiae). This phosphate can be transferred to the free OH of 2-phospho-D-glycerate, followed by transfer of the phosphate already on the phosphoglycerate back to the histidine. cf. EC 5.4.2.12 phosphoglycerate mutase. The enzyme has no requirement for metal ions. This enzyme also catalyse, slowly, the reactions of EC 5.4.2.4 bisphosphoglycerate mutase.
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Saccharomyces cerevisiae
UNIPROT: P00950
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Word Map
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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Synonyms
phosphoglycerate mutase, pgam1, phosphoglycerate mutase 1, sts-1, pgam2, cofactor-dependent phosphoglycerate mutase, dpgm-b, bisphosphoglycerate phosphatase, 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase, rv3214, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-phospho-D-glycerate = 3-phospho-D-glycerate
show the reaction diagram
SYSTEMATIC NAME
IUBMB Comments
D-phosphoglycerate 2,3-phosphomutase (2,3-diphosphoglycerate-dependent)
The enzymes from vertebrates, platyhelminths, mollusks, annelids, crustaceans, insects, algae, some fungi and some bacteria (particularly Gram-negative) require 2,3-bisphospho-D-glycerate as a cofactor. The enzyme is activated by 2,3-bisphospho-D-glycerate by transferring a phosphate to histidine (His10 in man and Escherichia coli, His8 in Saccharomyces cerevisiae). This phosphate can be transferred to the free OH of 2-phospho-D-glycerate, followed by transfer of the phosphate already on the phosphoglycerate back to the histidine. cf. EC 5.4.2.12 phosphoglycerate mutase. The enzyme has no requirement for metal ions. This enzyme also catalyse, slowly, the reactions of EC 5.4.2.4 bisphosphoglycerate mutase.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-phospho-D-glycerate
3-phospho-D-glycerate
show the reaction diagram
2-phospho-D-glycerate + 2,3-bisphosphoglycerate
3-phospho-D-glycerate + 2,3-bisphosphoglycerate
show the reaction diagram
2-Phosphoglycerate
3-Phosphoglycerate
show the reaction diagram
-
-
-
-
?
3-Phosphoglycerate
2-Phosphoglycerate
show the reaction diagram
-
-
-
-
?
3-Phosphoglycerate
?
show the reaction diagram
-
glycolysis/gluconeogenesis
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-phospho-D-glycerate
3-phospho-D-glycerate
show the reaction diagram
2-phospho-D-glycerate + 2,3-bisphosphoglycerate
3-phospho-D-glycerate + 2,3-bisphosphoglycerate
show the reaction diagram
-
-
-
r
3-Phosphoglycerate
?
show the reaction diagram
-
glycolysis/gluconeogenesis
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
benzene hexacarboxylate
-
benzene-1,2,3-tricarboxylate
-
benzene-1,2,4,5-tetracarboxylate
-
benzene-1,2,4-tricarboxylate
-
benzene-1,3,5-tricarboxylate
-
Inositol hexakisphosphate
-
2,3-Butanedione
-
-
diethyldicarbonate
-
-
Trinitrobenzenesulfonate
-
-
additional information
-
not Mg2+
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,3-bisphosphoglycerate
2,3-bisphosphoglycerate
-
-
2,3-diphosphoglycerate
2-phosphoglycollate
-
18-20fold activation of phosphatase activity
2-phosphohydroxypyruvate
-
30fold activation of phosphatase activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.43 - 1.1
3-phospho-D-glycerate
0.56
3-phosphoglycerate
-
0.041 - 0.067
2-phosphoglycerate
0.22 - 1.43
3-phospho-D-glycerate
0.026 - 0.74
3-phosphoglycerate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.7 - 530
3-phospho-D-glycerate
530
3-phosphoglycerate
-
0.0009 - 530
3-phospho-D-glycerate
0.078 - 490
3-phosphoglycerate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.006
benzene hexacarboxylate
-
0.023
benzene-1,2,3-tricarboxylate
-
0.013
benzene-1,2,4,5-tetracarboxylate
-
0.021
benzene-1,2,4-tricarboxylate
-
0.024
benzene-1,3,5-tricarboxylate
-
0.004
Inositol hexakisphosphate
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27000
-
4 * 27000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
tetramer
-
4 * 27000, SDS-PAGE
additional information
-
molecular dynamics simulation reveals that the enzyme interacts with its C-terminal domain with enolase, suggesting a direct transfer mechanism of substrate
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure at 2.12 a resolution
crystallization of PGAM complexed with inositol hexakisphosphate and benzene hexacarboxylate, crystal structures at 2.5-2.8 A resolution
hanging drop, 10 mg/ml ScPGM, 55% ammonium sulfate in 10 mM imidazole buffer, pH 6.8, 1 mM 3-phosphoglycerate, crystals of ScPGM complexed with 3-phosphoglycerate diffract to 1.7 A
sitting drop method, equal volumes of protein solution at a concentration of 10 mg/ml and well solution are mixed, well solution contains 60 mM Tris-HCl, pH 8.65, 120 mM lithium sulfate and 22-24% polyethylene glycol 4000, protein solution contains 1 mM inositol hexakisphosphate, crystals diffract to 2.3 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A60S
69% of wild-type activity
E86Q
1% of wild-type activity
S11A
4% of wild-type activity
H181A
-
His181 is substituted by Ala in site-directed mutagenesis. The resulting enzyme has a reduced activity and still requires 2,3-diphosphoglycerate. His181 seems to be important for cofactor-binding
K246G
-
mutant enzymes in which Ser11 is replaced by Gly, i.e. S11G and Lys246 by Gly, i.e. K246G do not have significantly altered kinetic values
L245G
-
39% of wild-type mutase activity, 111% of wild-type phosphatase activity
L245G/L246G
-
105% of wild-type mutase activity, 111% of wild-type phosphatase activity
L246G
-
98% of wild-type mutase activity, 122% of wild-type phosphatase activity
S11G
-
mutant enzymes in which Ser11 is replaced by Gly, i.e. S11G and Lys246 by Gly, i.e. K246G do not have significantly altered kinetic values
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55 - 60
-
neutral pH, presence of ammonium sulfate or 2,3-diphosphoglycerate, stable for several min
additional information
-
ammonium sulfate or 2,3-diphosphoglycerate stabilizes against elevated temperatures
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
loss of 45% of mutase activity after treatment with thermolysin
-
unstable to 8 M urea
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, CM cellulose, Superose 12
additional activities: bisphosphoglyceromutase, 2,3-diphosphoglycerophosphatase
-
recpmbinant PGAM
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Saccharomyces cerevisae
expression in Saccharomyces cerevisiae
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
renatured after denaturation with guanidine-HCl
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rose, Z.B.
The enzymology of 2,3-bisphosphoglycerate
Adv. Enzymol. Relat. Areas Mol. Biol.
51
211-253
1980
Saccharomyces cerevisiae, Gallus gallus, Oryctolagus cuniculus, Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Ray, W.J.; Peck, E.J.
Phosphomutases
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
6
407-477
1972
Saccharomyces cerevisiae, Gallus gallus, Oryctolagus cuniculus, Sus scrofa
-
Manually annotated by BRENDA team
Grisolia, S.
Phosphoglyceric acid mutases
Methods Enzymol.
5
236-242
1962
Saccharomyces cerevisiae
-
Manually annotated by BRENDA team
Rigden, D.J.; Alexeev, D.; Phillips, S.E.; Fothergill-Gilmore, L.A.
The 2.3 A X-ray crystal structure of S. cerevisiae phosphoglycerate mutase
J. Mol. Biol.
276
449-459
1998
Saccharomyces cerevisiae (P00950), Saccharomyces cerevisiae
Manually annotated by BRENDA team
White, M.F.; Fothergill-Gilmore, L.A.
Development of a mutagenesis, expression and purification system for yeast phosphoglycerate mutase
Eur. J. Biochem.
207
709-714
1992
Saccharomyces cerevisiae
Manually annotated by BRENDA team
White, M.; Fothergill-Gilmore L.A.
Mutase versus synthase: the phosphoglycerate mutase family studied by protein engineering
Biochem. Soc. Trans.
18
257
1990
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Johnson, C.M.; Price, N.C.
How similar are the phosphoglycerate mutases from yeast and rabbit muscle?
Biochem. Soc. Trans.
15
247-248
1987
Saccharomyces cerevisiae, Oryctolagus cuniculus
-
Manually annotated by BRENDA team
Sasaki, R.; Utsumi, S.; Sugimoto, E.; Chiba, H.
Subunit structure and multifunctional properties of yeast phosphoglyceromutase
Eur. J. Biochem.
66
523-533
1976
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Grisolia, S.; Carreras, J.
Phosphoglycerate mutase from yeast, chicken breast muscle, and kidney (2,3-PGA-dependent)
Methods Enzymol.
42
435-450
1975
Saccharomyces cerevisiae, Gallus gallus, Sus scrofa
Manually annotated by BRENDA team
Crowhurst, G.S.; Dalby, A.R.; Isupov, M.N.; Campbell, J.W.; Littlechild, J.A.
Structure of a phosphoglycerate mutase:3-phosphoglyceric acid complex at 1.7 A
Acta Crystallogr. Sect. D
55
1822-1826
1999
Saccharomyces cerevisiae (P00950), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Walter, R.A.; Nairn, J.; Duncan, D.; Price, N.C.; Kelly, S.M.; Rigden, D.J.; Fothergill-Gilmore, L.A.
The role of the C-terminal region in phosphoglycerate mutase
Biochem. J.
337
89-95
1999
Saccharomyces cerevisiae, Schizosaccharomyces pombe
-
Manually annotated by BRENDA team
Rigden, D.J.; Walter, R.A.; Phillips, S.E.; Fothergill-Gilmore, L.A.
Sulphate ions observed in the 2.12 A structure of a new crystal form of S. cerevisiae phosphoglycerate mutase provide insights into understanding the catalytic mechanism
J. Mol. Biol.
286
1507-1517
1999
Saccharomyces cerevisiae (P00950), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Rigden, D.J.; Walter, R.A.; Phillips, S.E.; Fothergill-Gilmore, L.A.
Polyanionic inhibitors of phosphoglycerate mutase: combined structural and biochemical analysis
J. Mol. Biol.
289
691-699
1999
Schizosaccharomyces pombe, Saccharomyces cerevisiae (P00950), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Hakobyan, D.; Nazaryan, K.
Investigation of interaction between enolase and phosphoglycerate mutase using molecular dynamics simulation
J. Biomol. Struct. Dyn.
23
625-633
2006
Saccharomyces cerevisiae
Manually annotated by BRENDA team