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Information on EC 2.7.1.41 - glucose-1-phosphate phosphodismutase
for references in articles please use BRENDA:EC2.7.1.41
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EC Tree 2 Transferases
2.7 Transferring phosphorus-containing groups
2.7.1 Phosphotransferases with an alcohol group as acceptor
2.7.1.41 glucose-1-phosphate phosphodismutase
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
showSynonyms
glucose-1-phosphate phosphodismutase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
glucose 1-phosphate transphosphorylase
-
-
-
-
PgcM
-
bifunctional PgcM with beta-phosphoglucomutase, EC 5.4.2.1, and glucose 1-phosphate phosphodismutase activities
phosphodismutase
-
-
-
-
phosphodismutase, glucose 1-phosphate
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 D-glucose 1-phosphate = D-glucose + D-glucose 1,6-bisphosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
D-glucose-1-phosphate:D-glucose-1-phosphate 6-phosphotransferase
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CAS REGISTRY NUMBER
COMMENTARY
9026-25-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alpha-D-glucose 1-phosphate + alpha-D-glucose 1-phosphate
alpha-D-glucose + alpha-D-glucose 1,6-bisphosphate
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose 1-phosphate + beta-D-glucose 1-phosphate
beta-D-glucose + beta-D-glucose 1,6-bisphosphate
-
Substrates: -
Products: -
Products: -
?
D-glucose 1-phosphate + D-glucose 1-phosphate
D-glucose + D-glucose 1,6-bisphosphate
-
Substrates: PgcM uses the alpha- and beta-forms of glucose 1-phosphate as substrates, higher affinity for the beta-form, binding of substrates and cofactors trigger a conformational change of PgcM
Products: -
Products: -
?
D-glucose 1-phosphate + D-glucose 1-phosphate
D-glucose + D-glucose 1,6-bisphosphate
-
Substrates: -
Products: -
Products: -
?
D-glucose 1-phosphate + D-glucose 1-phosphate
D-glucose + D-glucose 1,6-bisphosphate
-
Substrates: -
Products: -
Products: -
r
D-glucose 1-phosphate + D-glucose 1-phosphate
D-glucose + D-glucose 1,6-bisphosphate
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: bifunctional PgcM with beta-phosphoglucomutase, EC 5.4.2.1, and glucose 1-phosphate phosphodismutase activities
Products: -
Products: -
?
additional information
?
-
-
Substrates: carbohydrate metabolism
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
Substrates: carbohydrate metabolism
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
-
activation of forward reaction, optimal concentration: 1 mM, inhibition of reverse reaction, Mg2+ forms a complex with the product glucose-1,6-bisphosphate
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Mg2+
-
inhibits reverse reaction at 0.5 mM, forward reaction: activation
additional information
-
not inhibited by 8 mM fluoride, cysteine, histidine, adenylic acid or phosphate
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
forward reaction is not activated by ATP, cysteine, histidine, adenylic acid or phosphate
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
4 different enzymic activities of D-glucose 1,6-bisphosphate synthesis: in muscle glucose 1-phosphate transphosphorylase activity is the major activity, but not in brain
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
recombinant PgcM with beta-phosphoglucomutase and glucose 1-phosphate phosphodismutase activities
-
brenda
Highest Expressing Human Cell Lines
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
26500
-
3 * 26500, PgcM with beta-phosphoglucomutase and glucose 1-phosphate phosphodismutase activities, SDS-PAGE
28000
-
3 * 28000, PgcM with beta-phosphoglucomutase and glucose 1-phosphate phosphodismutase activities, estimated from the amino acid sequence data
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
trimer
trimer
-
3 * 28000, PgcM with beta-phosphoglucomutase and glucose 1-phosphate phosphodismutase activities, estimated from the amino acid sequence data
trimer
-
3 * 26500, PgcM with beta-phosphoglucomutase and glucose 1-phosphate phosphodismutase activities, SDS-PAGE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
95
-
30 min, stable, PgcM with beta-phosphoglucomutase and glucose 1-phosphate phosphodismutase activities
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable to 3-4 h dialysis against distilled water, prolonged or repeated dialysis inactivates
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
pgcM gene, encoding PgcM, a 226 amino acids protein with beta-phosphoglucomutase and glucose 1-phosphate phosphodismutase activities, is cloned, sequenced and used to construct a plasmid-based overexpression system for PcgM in Bacillus megaterium DSM 319
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sidbury, J.B.; Rosenberg, L.L.; Najjar, V.A.
Muscle glucose-1-phosphate transphosphorylase
J. Biol. Chem.
222
89-96
1956
Escherichia coli, Oryctolagus cuniculus
brenda
Climent, F.; Carreras, M.; Carreras, J.
Metabolism of glucose 1,6-diphosphate. I. Enzymes involved in the synthesis of glucose 1,6-diphosphate in pig tissues
Comp. Biochem. Physiol. B
81
737-742
1985
Sus scrofa
brenda
Mesak, L.R.; Dahl, M.K.
Purification and enzymatic characterization of PgcM: A beta-phosphoglucomutase and glucose-1-phosphate phosphodismutase of Bacillus subtilis
Arch. Microbiol.
174
256-264
2000
Bacillus subtilis
brenda
EXTERNAL LINKS (specific for EC-Number 2.7.1.41)
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