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Information on EC 5.4.2.11 - phosphoglycerate mutase (2,3-diphosphoglycerate-dependent) and Organism(s) Schizosaccharomyces pombe and UniProt Accession P36623

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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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Schizosaccharomyces pombe
UNIPROT: P36623
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The taxonomic range for the selected organisms is: Schizosaccharomyces pombe
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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[enzyme]-L-histidine
+
2,3-bisphospho-D-glycerate
=
[enzyme]-Ntau-phospho-L-histidine
+
3-phospho-D-glycerate
[enzyme]-L-histidine
+
=
[enzyme]-Ntau-phospho-L-histidine
+
2-phospho-D-glycerate
=
3-phospho-D-glycerate
=
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
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
-
-
r
2-phospho-D-glycerate
3-phospho-D-glycerate
show the reaction diagram
3-Phosphoglycerate
2-Phosphoglycerate
show the reaction diagram
-
-
-
-
?
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
-
-
r
2-phospho-D-glycerate
3-phospho-D-glycerate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,3-bisphosphoglycerate
-
required to prime the reaction in an initial phosphorylation step
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
-
-
diethyldicarbonate
-
-
Inositol hexakisphosphate
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,3-bisphosphoglycerate
-
-
2,3-diphosphoglycerate
-
-
2-phosphoglycollate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.58 - 7.46
3-phosphoglycerate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02 - 82
3-phospho-D-glycerate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.022
benzene hexacarboxylate
-
-
0.067
benzene-1,2,3-tricarboxylate
-
-
0.055
benzene-1,2,4,5-tetracarboxylate
-
-
0.062
benzene-1,2,4-tricarboxylate
-
-
0.053
benzene-1,3,5-tricarboxylate
-
-
0.035
Inositol hexakisphosphate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
210
-
chromosomal enzyme
218
-
recombinant enzyme
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23668
-
4 * 23678, chromosomal enzyme, 4 * 23669, mutants H196Q and H151Q, 4 * 23668, mutant H163Q, mass spectrometry
23669
-
4 * 23678, chromosomal enzyme, 4 * 23669, mutants H196Q and H151Q, 4 * 23668, mutant H163Q, mass spectrometry
23678
-
4 * 23678, chromosomal enzyme, 4 * 23669, mutants H196Q and H151Q, 4 * 23668, mutant H163Q, mass spectrometry
27000
-
4 * 27000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E93D
3D structure in solution obtained with NMR
E93D
-
less than 1% of wild-type activity
R120Q
-
59% of wild-type activity
R120Q/R121Q
-
62% of wild-type activity
R121Q
-
12% of wild-type activity
R14Q
-
less than 1% of wild-type activity
R94Q
-
1% of wild-type activity
S62A
-
loss of activity during purification
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
little effect of the protease thermolysin on enzyme activity
-
relatively resistant to short periods of treatment with thermolysin, both mutase and phosphatase activity decline at the same rate, approx. 40% loss of activity after 120 min treatment with thermolysin
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant PGAM
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Saccharomyces cerevisiae
expressed in Saccharomyces cerevisiae
-
expression in Saccharomyces cerevisiae
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Price, R.M.; Nairn, J.; Price, N.C.; Fothergill-Gilmore, L.A.
The reaction of phosphoglycerate mutase from Schizosaccharomyces pombe with diethylpyrocarbonate
Biochem. Soc. Trans.
24
324S
1996
Schizosaccharomyces pombe
Manually annotated by BRENDA team
Nairn, J.; Price, N.C.; Kelly, S.M.; Rigden, D.; Fothergill-Gilmore, L.A.; Krell, T.
Phosphoglycerate mutase from Schizosaccharomyces pombe: development of an expression system and characterisation of three histidine mutants of the enzyme
Biochim. Biophys. Acta
1296
69-75
1996
Schizosaccharomyces pombe
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
Nairn, J.; Duncan, D.; Price, N.E.; Kelly, S.M.; Fothergill-Gilmore, L.A.; Uhrinova, S.; Barlow, P.N.; Rigden, D.J.; Price, N.C.
Characterization of active-site mutants of Schizosaccharomyces pombe phosphoglycerate mutase. Elucidation of the roles of amino acids involved in substrate binding and catalysis
Eur. J. Biochem.
267
7065-7074
2000
Schizosaccharomyces pombe
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
Uhrinova, S.; Uhrin, D.; Nairn, J.; Price, N.C.; Fothergill-Gilmore, L.A.; Barlow, P.N.
Solution structure and dynamics of an open beta-sheet, glycolytic enzyme, monomeric 23.7 kDa phosphoglycerate mutase from Schizosaccharomyces pombe
J. Mol. Biol.
306
275-290
2001
Schizosaccharomyces pombe (P36623), Schizosaccharomyces pombe
Manually annotated by BRENDA team