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Information on EC 5.4.2.11 - phosphoglycerate mutase (2,3-diphosphoglycerate-dependent) and Organism(s) Sus scrofa

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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Sus scrofa
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The taxonomic range for the selected organisms is: Sus scrofa
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, rv3214, 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PGAM2
muscle-specific isoform
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
3-Phosphoglycerate
2-Phosphoglycerate
show the reaction diagram
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
tetrathionate
-
inactivation of MM-type isozyme, 50% of MB-type, BB-type not affected
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1 - 0.2
3-phosphoglycerate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
210
-
-
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
-
less than 50% of maximal activity above and below
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
Pgam2 is expressed at a high level in skeletal muscle during all the development stages
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A8D0M8T3_PIG
254
0
28848
TrEMBL
other Location (Reliability: 2)
B5KJG2_PIG
253
0
28677
TrEMBL
other Location (Reliability: 3)
A0A4X1VRK0_PIG
226
0
26647
TrEMBL
other Location (Reliability: 3)
A0A4X1VTD9_PIG
259
0
29939
TrEMBL
other Location (Reliability: 3)
A0A4X1UA74_PIG
254
0
28804
TrEMBL
other Location (Reliability: 2)
A0A8D0QR32_PIG
253
0
28677
TrEMBL
other Location (Reliability: 3)
A0A8D0Z3F2_PIG
262
0
29711
TrEMBL
other Location (Reliability: 2)
A0A286ZQ31_PIG
259
0
29939
TrEMBL
other Location (Reliability: 3)
A0A8D1I1J2_PIG
253
0
28659
TrEMBL
other Location (Reliability: 3)
A0A4X1U986_PIG
252
0
28564
TrEMBL
other Location (Reliability: 3)
A0A287AJQ2_PIG
254
0
28804
TrEMBL
other Location (Reliability: 2)
B5KJG3_PIG
23
0
2591
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28680
calculated from amino acid sequence
29000
-
2 * 29000, SDS-PAGE
57000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 29000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55 - 60
-
neutral pH, presence of ammonium sulfate or 2,3-diphosphoglycerate, stable for several min
60
-
MM-type isozyme very stable, BB-type and MB-type are inactivated rapidly, 2,3-diphosphoglycerate protects
additional information
-
ammonium sulfate or 2,3-diphosphoglycerate stabilizes against elevated temperatures
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
MM-type, BB-type, MB-type isozymes, these enzymes also show glycerate 2,3-diphosphate synthase and glycerate 2,3-diphosphate phosphatase activity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in PK-15 cells
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
Kulbe, K.D.; Foellmer, H.; Fuchs, J.
Simultaneous purification of glyceraldehyde-3-phosphate dehydrogenase, 3-phosphoglycerate kinase, and phosphoglycerate mutase from pig liver and muscle
Methods Enzymol.
90
498-511
1982
Sus scrofa
Manually annotated by BRENDA team
Bartrons, R.; Carreras, J.
Purification and characterization of phosphoglycerate mutase isozymes from pig heart
Biochim. Biophys. Acta
708
167-177
1982
Sus scrofa
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
Qiu, H.; Zhao, S.; Xu, X.; Yerle, M.; Liu, B.
Assignment and expression patterns of porcine muscle-specific isoform of phosphoglycerate mutase gene
J. Genet. Genomics
35
257-260
2008
Sus scrofa (B5KJG2), Sus scrofa (B5KJG3), Sus scrofa
Manually annotated by BRENDA team