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Enzyme Nomenclature
Information on EC 5.4.2.2 - phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent)
for references in articles please use BRENDA:EC5.4.2.2
Word Map on EC 5.4.2.2
- 5.4.2.2
- hexokinase
- starch
- malate
- glycogen
-
phosphorylase
- 6-phosphogluconate
- adenylate
-
esterase
-
pyrophosphorylase
- erythrocyte
- 1-phosphate
- glucose-1-phosphate
- gpi
-
aldolase
-
phosphofructokinase
- isocitrate
-
transferrin
-
allozyme
-
haptoglobin
-
malic
-
glucosephosphate
-
hardy-weinberg
- glyoxalase
- phosphoglucoisomerase
-
monomorphic
- entamoeba
- histolytica
-
zymodemes
- glucose-6-phosphatase
- diptera
- adp-glucose
-
phosphohexose
- fructokinase
-
starch-gel
- plastidial
-
glc-6-p
-
5.3.1.9
-
bloodstain
- galactose-1-phosphate
-
duffy
-
glycogenolysis
-
phosphoenzyme
-
uridylyltransferase
- udp-galactose
-
leloir
- 1,6-diphosphate
-
isoenzymatic
- udp-glc
-
2.7.1.1
- amyloplasts
- food industry
- medicine
- molecular biology
- drug development
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
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EC NUMBER 
COMMENTARY 
5.4.2.2
-
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RECOMMENDED NAME
GeneOntology No.
phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
alpha-D-glucose 1-phosphate = D-glucose 6-phosphate
in the forward reaction a phosphate from the enzyme is transferred to C-6 of glucose 1-phosphate which results in a dephosphoenzyme intermediate. In the second step phosphate from the C-1 of glucose is transferred to the enzyme for its regeneration. The reverse reaction proceeds via a similar mechanism
-
alpha-D-glucose 1-phosphate = D-glucose 6-phosphate
ping-pong mechanism
-
alpha-D-glucose 1-phosphate = D-glucose 6-phosphate
acid-base catalysis mechanism, overview. His329 is appropriately positioned to abstract a proton from the O1/O6 hydroxyl of the phosphosugar substrates, and thus may serve as the general base in the reaction
-
alpha-D-glucose 1-phosphate = D-glucose 6-phosphate
acid-base catalysis mechanism, key role for conformational change in its multistep reaction, which requires a dramatic 180 degree reorientation of the intermediate within the active site. Modeling shows that increased enzyme flexibility facilitates the reorientation of the reaction intermediate, coupling changes in structural dynamics with the unique catalytic mechanism of this enzyme
-
alpha-D-glucose 1-phosphate = D-glucose 6-phosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
group transfer
-
-
intramolecular, phosphate group
-
isomerization
isomerization
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
alpha-D-glucose 1,6-phosphomutase
Maximum activity is only obtained in the presence of alpha-D-glucose 1,6-bisphosphate. This bisphosphate is an intermediate in the reaction, being formed by transfer of a phosphate residue from the enzyme to the substrate, but the dissociation of bisphosphate from the enzyme complex is much slower than the overall isomerization. The enzyme also catalyses (more slowly) the interconversion of 1-phosphate and 6-phosphate isomers of many other alpha-D-hexoses, and the interconversion of alpha-D-ribose 1-phosphate and 5-phosphate. cf. EC 5.4.2.5, phosphoglucomutase (glucose-cofactor).
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CAS REGISTRY NUMBER
COMMENTARY
9001-81-4
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform PGM-2, enzyme mRNA expression is mostly up-regulated in the first steps of the response to pollutant exposure and is xenobiotic-dependent
Uniprot
no activity in Trypanosoma brucei
the organism lost the PGM gene, activity is catalyzed by phosphomannomutase, EC 5.4.2.8 and phospho-N-acetylglucosamine mutase, EC 5.4.2.3
-
-
serovar typhimurium
UniProt
syncytia induced by nematode Heterodera schachtii
UniProt
rabbit
-
-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
the enzyme belongs to the alpha-D-phosphohexomutase enzyme superfamily
malfunction
metabolism
physiological function
additional information
malfunction
-
targeted deletion of pgmA in Yersinia pestis strain KIM5 results in loss of autoaggregation, the deletion mutant displays more than 1000fold increased sensitivity to polymyxin B compared to the parental strain
malfunction
the pgm deletion mutant has impaired growth in vitro, is deficient in the ability to utilize alpha-D-galactose as a carbon source and displays reduced O-antigen polymer length
malfunction
-
whereas pgm2 and pgm3 single mutants are undistinguishable from the wild type, loss of both PGM2 and PGM3 severely impairs male and female gametophyte function. Double mutant pollen completes development but fails to germinate, double mutant ovules also develop normally, but approximately half remain unfertilized 2 d after pollination
malfunction
-
only mutants with a deletion of PGM3, not of PGM1 or PGM2, hyperaccumulate ribose-1-phosphate
malfunction
-
whereas pgm2 and pgm3 single mutants are undistinguishable from the wild type, loss of both PGM2 and PGM3 severely impairs male and female gametophyte function. Double mutant pollen completes development but fails to germinate, double mutant ovules also develop normally, but approximately half remain unfertilized 2 d after pollination
-
malfunction
-
the pgm deletion mutant has impaired growth in vitro, is deficient in the ability to utilize alpha-D-galactose as a carbon source and displays reduced O-antigen polymer length
-
malfunction
-
targeted deletion of pgmA in Yersinia pestis strain KIM5 results in loss of autoaggregation, the deletion mutant displays more than 1000fold increased sensitivity to polymyxin B compared to the parental strain
-
metabolism
-
PGM is a key enzyme in carbohydrate metabolism, where it catalyzes the reversible transfer of a phosphate group between C-1 and C-6 of D-glucose via D-glucose 1,6-diphosphate
metabolism
-
cytosolic PGM activity is not limiting for carbon metabolism
metabolism
-
cytosolic PGM activity is not limiting for carbon metabolism
-
metabolism
-
PGM is a key enzyme in carbohydrate metabolism, where it catalyzes the reversible transfer of a phosphate group between C-1 and C-6 of D-glucose via D-glucose 1,6-diphosphate
-
physiological function
-
PgmA is required for efficient autoaggregation in Yersinia pestis and plays an important role in antimicrobial peptide resistance
physiological function
Pgm is required by Salmonella enterica serovar Typhimurium for O-antigen production, resistance to antimicrobial peptides, and in vivo fitness
physiological function
-
overexpression of pgm gene has no significant effect on UDP-glucose and UDP-galactose levels and increased alpha-Pgm activity does not significantly change the lactate production
physiological function
-
pollen germination requires cytosolic PGM activity
physiological function
-
Unlike the majority of alpha-phosphoglucomutases, the described enzyme of 252 residues with alpha-phosphoglucomutase activity, is related to eukaryotic phosphomannomutases and belongs to HAD-superfamily hydrolase, subfamily IIB.
physiological function
the enzyme is involved in biosynthesis of sphingans, extracellular polysaccharides
physiological function
-
the enzyme is involved in glycogen catabolism
physiological function
-
the enzyme catalyzes an intramolecular phosphoryl transfer across its phosphosugar substrates, which are precursors in the synthesis of exoproducts involved in bacterial virulence
physiological function
-
the plastidial PGM limits photosynthetic carbon flow into starch
physiological function
the enzyme plays an important role in polysaccharide capsule formation and virulence in a number of bacterial pathogens
physiological function
-
pollen germination requires cytosolic PGM activity
-
physiological function
-
the enzyme plays an important role in polysaccharide capsule formation and virulence in a number of bacterial pathogens
-
physiological function
-
Pgm is required by Salmonella enterica serovar Typhimurium for O-antigen production, resistance to antimicrobial peptides, and in vivo fitness
-
physiological function
-
the enzyme is involved in biosynthesis of sphingans, extracellular polysaccharides
-
physiological function
-
PgmA is required for efficient autoaggregation in Yersinia pestis and plays an important role in antimicrobial peptide resistance
-
additional information
-
analysis of conformational flexibility of different forms of phosphoglucomutase/phosphomannomutase in solution, including its active, phosphorylated state and the unphosphorylated state that occurs transiently during the catalytic cycle, by hydrogen-deuterium exchange by mass spectrometry and small angle x-ray scattering. Both ligand binding and phosphorylation of the catalytic phosphoserine affect the overall flexibility of the enzyme in solution
additional information
structure homology modeling, overview
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alpha-D-glucose 6-phosphate
alpha-D-glucose 1-phosphate
23% of the activity with alpha-D-glucose 1-phosphate
-
-
r
D-fructose-1-phosphate
D-fructose-6-phosphate
-
no mutase activity
-
-
?
D-glucosamine-1-phosphate
D-glucosamine-6-phosphate
-
low enzyme activity
-
-
?
D-glucose 1-phosphate + D-fructose 1,6-diphosphate
D-glucose 1,6-diphosphate + D-fructose 1-phosphate + D-fructose 6-phosphate
-
synthesis of glucose 1,6-diphosphate is an additional activity
synthesis of glucose 1,6-diphosphate is an additional activity
-
Glucose 1-phosphate + 1,3-bisphosphoglycerate
Glucose 1,6-diphosphate + glycerate 3-phosphate
-
synthesis of glucose 1,6-diphosphate is an additional activity
synthesis of glucose 1,6-diphosphate is an additional activity
-
N-acetyl-D-glucosamine-1-phosphate
N-acetyl-D-glucosamine-6-phosphate
-
no mutase activity
-
-
?
alpha-D-glucose 1-phosphate
?
-
key enzyme in carbohydrate metabolism
-
-
-
alpha-D-glucose 1-phosphate
?
-
degradation of lactose in lactic acid bacteria
-
-
-
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
-
-
-
r
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
-
-
-
?
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
the beta-form is inactive
-
-
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
enzyme is highly specific for substrate and product
-
-
r
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
the forward reaction is faster than the reverse reaction
-
-
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
the beta-form is inactive
-
-
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
-
-
r
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
-
-
r
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
-
r
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
-
-
-
?
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
-
-
-
?
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
-
-
-
?
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
-
-
?
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
-
-
r
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
-
-
?
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
-
-
r
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
SP-1 shows preference for glucose-1-phosphate rather than mannose-1-phosphate
-
-
?
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
SP-1 shows preference for glucose-1-phosphate rather than mannose-1-phosphate
-
-
?
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
-
-
?
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
-
-
?
alpha-D-glucose 1-phosphate
D-glucose 6-phosphate
-
-
-
r
alpha-D-glucose 1-phosphate
D-glucose 6-phosphate
-
-
-
?
alpha-D-glucose 1-phosphate
D-glucose 6-phosphate
it is unclear whether either glucose or mannose phosphate represents the cellular substrate for SsoPHM. The Km values for rSsoPHM toward glucose 6-phosphate and mannose 6-phosphate are in the low millimolar range, significantly higher than that expected for a physiological substrate. Since the protein encoded by sso0207 is the only identifiable phosphohexomutase in the Sulfolbus solfataricus P2 genome, SsoPHM provides the only recognizable avenue for interconverting glucose 6-phosphate and glucose 1-phosphate during glycogen synthesis and breakdown
-
-
r
alpha-D-glucose 1-phosphate
D-glucose 6-phosphate
the enzyme also catalyzes the interconversion of alpha-D-mannose 1-phosphate and D-mannose 6-phosphate
-
-
r
alpha-D-glucose 1-phosphate
D-glucose 6-phosphate
it is unclear whether either glucose or mannose phosphate represents the cellular substrate for SsoPHM. The Km values for rSsoPHM toward glucose 6-phosphate and mannose 6-phosphate are in the low millimolar range, significantly higher than that expected for a physiological substrate. Since the protein encoded by sso0207 is the only identifiable phosphohexomutase in the Sulfolbus solfataricus P2 genome, SsoPHM provides the only recognizable avenue for interconverting glucose 6-phosphate and glucose 1-phosphate during glycogen synthesis and breakdown
-
-
r
alpha-D-glucose 1-phosphate
D-glucose 6-phosphate
the enzyme also catalyzes the interconversion of alpha-D-mannose 1-phosphate and D-mannose 6-phosphate
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
-
-
-
?
alpha-D-mannose 1-phosphate
D-mannose-6-phosphate
SP-1 shows preference for glucose-1-phosphate rather than mannose-1-phosphate
-
-
?
alpha-D-mannose 1-phosphate
D-mannose-6-phosphate
SP-1 shows preference for glucose-1-phosphate rather than mannose-1-phosphate
-
-
?
D-glucose 6-phosphate
alpha-D-glucose 1-phosphate
it is unclear whether either glucose or mannose phosphate represents the cellular substrate for SsoPHM. The Km values for rSsoPHM toward glucose 6-phosphate and mannose 6-phosphate are in the low millimolar range, significantly higher than that expected for a physiological substrate. Since the protein encoded by sso0207 is the only identifiable phosphohexomutase in the Sulfolbus solfataricus P2 genome, SsoPHM provides the only recognizable avenue for interconverting glucose 6-phosphate and glucose 1-phosphate during glycogen synthesis and breakdown
-
-
r
D-glucose 6-phosphate
alpha-D-glucose 1-phosphate
the enzyme also catalyzes the interconversion of alpha-D-mannose 1-phosphate and D-mannose 6-phosphate. No activity toward glucosamine 6-phosphate or N-acetylglucosamine 6-phosphate
-
-
r
D-glucose 6-phosphate
alpha-D-glucose 1-phosphate
it is unclear whether either glucose or mannose phosphate represents the cellular substrate for SsoPHM. The Km values for rSsoPHM toward glucose 6-phosphate and mannose 6-phosphate are in the low millimolar range, significantly higher than that expected for a physiological substrate. Since the protein encoded by sso0207 is the only identifiable phosphohexomutase in the Sulfolbus solfataricus P2 genome, SsoPHM provides the only recognizable avenue for interconverting glucose 6-phosphate and glucose 1-phosphate during glycogen synthesis and breakdown
-
-
r
D-glucose 6-phosphate
alpha-D-glucose 1-phosphate
the enzyme also catalyzes the interconversion of alpha-D-mannose 1-phosphate and D-mannose 6-phosphate. No activity toward glucosamine 6-phosphate or N-acetylglucosamine 6-phosphate
-
-
r
D-glucose-1-phosphate
D-glucose-6-phosphate
-
bifunctional enzyme
-
-
?
D-mannose-1-phosphate
D-mannose-6-phosphate
-
bifunctional enzyme
-
-
?
Glucose 6-phosphate
?
-
synthesis of glucose 1-phosphate for the formation of UDPglucose
-
-
-
additional information
?
-
-
isozyme PGM2 also displays activities of phosphoribomutase and glucose 1,6-bisphosphate synthase
-
-
-
additional information
?
-
-
isozyme PGM2 also displays activities of phosphoribomutase and glucose 1,6-bisphosphate synthase
-
-
-
additional information
?
-
-
no substrate: alpha-D-mannose 1-phosphate, beta-D-glucose 1-phosphate
-
-
-
additional information
?
-
no substrate: alpha-D-mannose 1-phosphate, beta-D-glucose 1-phosphate
-
-
-
additional information
?
-
-
bifunctional enzyme with phosphoglucomutase and phosphomannomutase, EC 5.4.2.8, activities
-
-
-
additional information
?
-
-
bifunctional enzyme with phosphoglucomutase and phosphomannomutase, EC 5.4.2.8, activities. Strongly conserved residue His329 in the active site is critical for enzyme activity. His329 is appropriately positioned to abstract a proton from the O1/O6 hydroxyl of the phosphosugar substrates, and thus may serve as the general base in the reaction
-
-
-
additional information
?
-
-
PGM from Clostridium thermocellum is a dual-specificity enzyme with phosphoglucomutase and phosphomannomutase activities
-
-
-
additional information
?
-
-
no activity with alpha-D-ribose 5-phosphate
-
-
-
additional information
?
-
-
Pgm3 functions as the major phosphoribomutase in vivo
-
-
-
additional information
?
-
-
phosphoglucomutases Pgm1, Pgm2, and Pgm3, EC 5.4.2.2, of Saccharomyces cerevisiae show ability to interconvert ribose-1-phosphate and ribose-5-phosphate. The purified proteins, studied in vitro with regard to their kinetic properties on glucose-1-phosphate and ribose-1-phosphate, are all active on both substrates with Pgm1 exhibiting only residual activity on ribose-1-phosphate. The Pgm2 and Pgm3 proteins have almost equal kinetic properties on ribose-1-phosphate, but Pgm2 has a 2000times higher preference for glucose-1-phosphate when compared to Pgm3
-
-
-
additional information
?
-
-
no activity with alpha-D-ribose 5-phosphate
-
-
-
additional information
?
-
bifunctional enzyme with phosphoglucomutase and phosphomannomutase, EC 5.4.2.8, activities, the catalytic efficiency is about 15fold higher for glucose 1-phosphate than for mannose 1-phosphate
-
-
-
additional information
?
-
-
bifunctional enzyme with phosphoglucomutase and phosphomannomutase, EC 5.4.2.8, activities, the catalytic efficiency is about 15fold higher for glucose 1-phosphate than for mannose 1-phosphate
-
-
-
additional information
?
-
bifunctional enzyme with phosphoglucomutase and phosphomannomutase, EC 5.4.2.8, activities, the catalytic efficiency is about 15fold higher for glucose 1-phosphate than for mannose 1-phosphate
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alpha-D-glucose 1-phosphate
?
-
key enzyme in carbohydrate metabolism
-
-
-
alpha-D-glucose 1-phosphate
?
-
degradation of lactose in lactic acid bacteria
-
-
-
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
-
-
r
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
-
-
r
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
P26276
-
-
r
alpha-D-glucose 1-phosphate
D-glucose 6-phosphate
I6Y2G3
-
-
-
r
alpha-D-glucose 1-phosphate
D-glucose 6-phosphate
M1T754
-
-
-
?
alpha-D-glucose 1-phosphate
D-glucose 6-phosphate
Q980S1
it is unclear whether either glucose or mannose phosphate represents the cellular substrate for SsoPHM. The Km values for rSsoPHM toward glucose 6-phosphate and mannose 6-phosphate are in the low millimolar range, significantly higher than that expected for a physiological substrate. Since the protein encoded by sso0207 is the only identifiable phosphohexomutase in the Sulfolbus solfataricus P2 genome, SsoPHM provides the only recognizable avenue for interconverting glucose 6-phosphate and glucose 1-phosphate during glycogen synthesis and breakdown
-
-
r
alpha-D-glucose 1-phosphate
D-glucose 6-phosphate
Q980S1
it is unclear whether either glucose or mannose phosphate represents the cellular substrate for SsoPHM. The Km values for rSsoPHM toward glucose 6-phosphate and mannose 6-phosphate are in the low millimolar range, significantly higher than that expected for a physiological substrate. Since the protein encoded by sso0207 is the only identifiable phosphohexomutase in the Sulfolbus solfataricus P2 genome, SsoPHM provides the only recognizable avenue for interconverting glucose 6-phosphate and glucose 1-phosphate during glycogen synthesis and breakdown
-
-
r
D-glucose 6-phosphate
alpha-D-glucose 1-phosphate
Q980S1
it is unclear whether either glucose or mannose phosphate represents the cellular substrate for SsoPHM. The Km values for rSsoPHM toward glucose 6-phosphate and mannose 6-phosphate are in the low millimolar range, significantly higher than that expected for a physiological substrate. Since the protein encoded by sso0207 is the only identifiable phosphohexomutase in the Sulfolbus solfataricus P2 genome, SsoPHM provides the only recognizable avenue for interconverting glucose 6-phosphate and glucose 1-phosphate during glycogen synthesis and breakdown
-
-
r
D-glucose 6-phosphate
alpha-D-glucose 1-phosphate
Q980S1
it is unclear whether either glucose or mannose phosphate represents the cellular substrate for SsoPHM. The Km values for rSsoPHM toward glucose 6-phosphate and mannose 6-phosphate are in the low millimolar range, significantly higher than that expected for a physiological substrate. Since the protein encoded by sso0207 is the only identifiable phosphohexomutase in the Sulfolbus solfataricus P2 genome, SsoPHM provides the only recognizable avenue for interconverting glucose 6-phosphate and glucose 1-phosphate during glycogen synthesis and breakdown
-
-
r
Glucose 6-phosphate
?
-
synthesis of glucose 1-phosphate for the formation of UDPglucose
-
-
-
additional information
?
-
-
bifunctional enzyme with phosphoglucomutase and phosphomannomutase, EC 5.4.2.8, activities
-
-
-
additional information
?
-
-
bifunctional enzyme with phosphoglucomutase and phosphomannomutase, EC 5.4.2.8, activities. Strongly conserved residue His329 in the active site is critical for enzyme activity. His329 is appropriately positioned to abstract a proton from the O1/O6 hydroxyl of the phosphosugar substrates, and thus may serve as the general base in the reaction
-
-
-
additional information
?
-
-
Pgm3 functions as the major phosphoribomutase in vivo
-
-
-
additional information
?
-
M1T754
bifunctional enzyme with phosphoglucomutase and phosphomannomutase, EC 5.4.2.8, activities, the catalytic efficiency is about 15fold higher for glucose 1-phosphate than for mannose 1-phosphate
-
-
-
additional information
?
-
-
bifunctional enzyme with phosphoglucomutase and phosphomannomutase, EC 5.4.2.8, activities, the catalytic efficiency is about 15fold higher for glucose 1-phosphate than for mannose 1-phosphate
-
-
-
additional information
?
-
M1T754
bifunctional enzyme with phosphoglucomutase and phosphomannomutase, EC 5.4.2.8, activities, the catalytic efficiency is about 15fold higher for glucose 1-phosphate than for mannose 1-phosphate
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Mg2+
Mn2+
Ni2+
additional information
Ca2+
-
the enzyme is also active with 5 mM Ca2+ but to a lesser extent as Co2+ (11.9% relative activity)
Co2+
-
PGM requires the presence of a divalent cation for its function with maximum activity (100%) being obtained with 5 mM Co2+
Mg2+
-
the enzyme is also active with 5 mM Mg2+ but to a lesser extent as Co2+ (24.5% relative activity)
Mg2+
Mg2+ are the most effective divalent cations for the enzyme activity of isozyme PGM-I; Mg2+ are the most effective divalent cations for the enzyme activity of isozyme PGM-II
Mn2+
-
the enzyme is also active with 5 mM Mn2+ but to a lesser extent as Co2+ (69.5% relative activity)
Mn2+
a single Mg2+ ion is required for catalytic activity, each PGM monomer contains one bound Mg2+ ion in its metal binding site
Ni2+
-
the enzyme is also active with 5 mM Ni2+ but to a lesser extent as Co2+ (22.5% relative activity)
additional information
-
no detectable activity after addition of 0.1 mM EDTA
additional information
-
Zn2+, Cu2+ and Pd2+ do not enhance the PGM activity
additional information
PGM activity of SP-1 requires divalent metal ions
additional information
-
PGM activity of SP-1 requires divalent metal ions
additional information
-
Ni2+, Mn2+ and Zn2+ at a concentration of 1 mM can also support activity, although to a lesser extent
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Disperse Blue 56
-
kinetic studies indicate that it is a parabolic, noncompetitive inhibitor. Reduction of the inhibition in the presence of 0.01% Triton X-100
additional information
-
not inhibitory: 1,5-diamino-4,8-dihydroxyanthraquinone
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
alpha-D-Glucose 1,6-bisphosphate
the maximum activity is obtained in the presence of more than 0.2 mM alpha-D-glucose 1,6-bisphosphate; the maximum activity is obtained in the presence of more than 0.2 mM alpha-D-glucose 1,6-bisphosphate
Imidazol
-
addition at concentrations below that of Mg2+ increases the activity
alpha-D-glucose 1,6-diphosphate
-
Km: 0.00053 mM phosphoglucomutase I, 0.00232 mM, phosphoglucomutase II
alpha-D-glucose 1,6-diphosphate
-
peak I enzyme Km: 0.0018 mM; peak II enzyme, Km: 0.0022 mM
additional information
-
high pullulan yield is related to high activities of alpha-phosphoglucose mutase
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00103
D-glucose 1,6-diphosphate
-
in 41 mM 1,3-diaza-2,4-cyclopentadiene /HCl (pH 7.6), 5 mM MgCl2, at 25°C
0.0013
alpha-D-glucose 1-phosphate
H308N/H329N double mutant; S108A mutant
0.003
alpha-D-glucose 1-phosphate
-
PGM2, in 50 mM HEPES, pH 7.1, 5 mM MgCl2, at 30°C
0.0082
alpha-D-glucose 1-phosphate
-
PGM1, in 50 mM HEPES, pH 7.1, 5 mM MgCl2, at 30°C
0.026
alpha-D-glucose 1-phosphate
-
recombinant His-tagged Pgm2, pH 7.5, 30°C
0.03
alpha-D-glucose 1-phosphate
-
mutant H329A, pH 7.5, temperature not specified in the publication
0.06
alpha-D-glucose 1-phosphate
-
recombinant His-tagged Pgm1, pH 7.5, 30°C
0.08
alpha-D-glucose 1-phosphate
-
wild-type enzyme, pH 7.5, temperature not specified in the publication
0.1
alpha-D-glucose 1-phosphate
-
in 41 mM 1,3-diaza-2,4-cyclopentadiene /HCl (pH 7.6), 5 mM MgCl2, at 25°C
0.1 - 2
alpha-D-glucose 1-phosphate
recombinant enzyme, pH 7.4, 30°C
0.112
alpha-D-glucose 1-phosphate
-
recombinant His-tagged Pgm3, pH 7.5, 30°C
0.19
alpha-D-glucose 1-phosphate
isozyme PGM-I, in 50 mM HEPES-KOH, pH 8.0, at 37°C
0.2 - 1
alpha-D-glucose 1-phosphate
recombinant His-tagged enzyme, pH 7.6, temperature not specified in the publication
0.2228
alpha-D-glucose 1-phosphate
SP-1, in 50 mM Tris-HCl (pH 7.5), at 37°C
0.41
alpha-D-glucose 1-phosphate
-
recombinant wild type enzyme, at 60°C
3.53
alpha-D-glucose 1-phosphate
isozyme PGM-II, in 50 mM HEPES-KOH, pH 8.0, at 37°C
0.4392
alpha-D-mannose 1-phosphate
SP-1, in 50 mM Tris-HCl (pH 7.5), at 37°C
0.44
alpha-D-mannose 1-phosphate
-
recombinant wild type enzyme, at 60°C
8
D-glucose 6-phosphate
pH 6.5, 65°C, mutant enzyme S309N; pH 6.5, 65°C, mutant enzyme S309T
additional information
additional information
-
KM mannose-1-phosphate isoenzyme PH0923S101A not detectable, 37°C
-
additional information
additional information
-
Michaelis-Menten steady-state kinetics of wild-type and mutant H329A enzymes, overview
-
additional information
additional information
Michaelis-Menten kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.74
D-glucose 1,6-diphosphate
-
in 41 mM 1,3-diaza-2,4-cyclopentadiene /HCl (pH 7.6), 5 mM MgCl2, at 25°C
0.03
alpha-D-glucose 1-phosphate
-
mutant H329A, pH 7.5, temperature not specified in the publication
0.74
alpha-D-glucose 1-phosphate
-
in 41 mM 1,3-diaza-2,4-cyclopentadiene /HCl (pH 7.6), 5 mM MgCl2, at 25°C
10.77
alpha-D-glucose 1-phosphate
recombinant His-tagged enzyme, pH 7.6, temperature not specified in the publication
70.31
alpha-D-glucose 1-phosphate
recombinant enzyme, pH 7.4, 30°C
93
alpha-D-glucose 1-phosphate
isozyme PGM-II, in 50 mM HEPES-KOH, pH 8.0, at 37°C
95
alpha-D-glucose 1-phosphate
-
wild-type enzyme, pH 7.5, temperature not specified in the publication
126.8
alpha-D-glucose 1-phosphate
SP-1, in 50 mM Tris-HCl (pH 7.5), at 37°C
190
alpha-D-glucose 1-phosphate
-
recombinant wild type enzyme, at 60°C
398
alpha-D-glucose 1-phosphate
isozyme PGM-I, in 50 mM HEPES-KOH, pH 8.0, at 37°C
59
alpha-D-mannose 1-phosphate
-
recombinant wild type enzyme, at 60°C
79.17
alpha-D-mannose 1-phosphate
SP-1, in 50 mM Tris-HCl (pH 7.5), at 37°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
714.3
D-glucose 1,6-diphosphate
-
in 41 mM 1,3-diaza-2,4-cyclopentadiene /HCl (pH 7.6), 5 mM MgCl2, at 25°C
1
alpha-D-glucose 1-phosphate
-
mutant H329A, pH 7.5, temperature not specified in the publication
7.38
alpha-D-glucose 1-phosphate
-
in 41 mM 1,3-diaza-2,4-cyclopentadiene /HCl (pH 7.6), 5 mM MgCl2, at 25°C
51.27
alpha-D-glucose 1-phosphate
recombinant His-tagged enzyme, pH 7.6, temperature not specified in the publication
58.4
alpha-D-glucose 1-phosphate
recombinant enzyme, pH 7.4, 30°C
1188
alpha-D-glucose 1-phosphate
-
wild-type enzyme, pH 7.5, temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.23
D-Glucose 1,6-bisphosphate
-
25°C, pH 7.6, substrate inhibition at high concentrations
3.3
D-glucose 1-phosphate
-
25°C, pH 7.6, substrate inhibition at high concentrations
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
76
-
PGM2, using alpha-D-glucose 1-phosphate as substrate, in 50 mM HEPES, pH 7.1, 5 mM MgCl2, at 30°C
84
isozyme PGM-II, using alpha-D-glucose 1-phosphate as substrate, in 50 mM HEPES-KOH, pH 8.0, at 37°C
87
-
PGM1, using alpha-D-glucose 1-phosphate as substrate, in 50 mM HEPES, pH 7.1, 5 mM MgCl2, at 30°C
338
isozyme PGM-I, using alpha-D-glucose 1-phosphate as substrate, in 50 mM HEPES-KOH, pH 8.0, at 37°C
additional information
additional information
-
isoenzyme PH0923 PGM Vmax 24, 65°C; isoenzyme PH0923 PMM Vmax 0.7, 37°C; isoenzyme PH0923S101A PGM Vmax 0.4, 65°C; isoenzyme PH0923S101A PMM Vmax not detectable, 37°C
additional information
-
PGM activity decreases more than fivefold in mutant TnM2 compared to the wild type strain
additional information
-
2-deoxyribose-1-phosphate Vmax 0.230, 90°C; D-glucose-1-phosphate Vmax 0.690, 90°C, pH 7.0; D-mannose-1-phosphate Vmax 0.401, 90°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
7.5
7.5
7.9
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8
-
using 3-(N-morpholino)propanesulfonic acid buffer, the enzyme retains up to 90% of its initial activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
inhibition of phosphoglucomutase activity by chronic treatment with Li+ causes alterations of glucose-phosphate level with compensatory elevation of phosphoglucomutase activity
-
inhibition of phosphoglucomutase activity by chronic treatment with Li+ causes compensatory elevation of phosphoglucomutase activity in Li+-treated bipolar patients due to increased expression of PGM1 gene
-
inhibition of phosphoglucomutase activity by chronic treatment with Li+ causes alterations of glucose-phosphate level with compensatory elevation of phosphoglucomutase activity
-
-
-
skeletal muscle and cardiac muscle, inhibition of phosphoglucomutase activity by chronic treatment with Li+ causes alterations of glucose-phosphate level with compensatory elevation of phosphoglucomutase activity
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
associated with phospholipids and/or phosphoproteins
-
isoforms PGM2 and PGM3
-
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Lactococcus lactis subsp. cremoris (strain MG1363)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
Xanthomonas axonopodis pv. citri (strain 306)
Q8PGN7
Xanthomonas axonopodis pv. citri (strain 306)
Q8PGN7
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
31633
-
2 * 31633, sedimentation equilibrium in 6 M guanidine-HCl, sedimentation equilibrium in dodecyl sulfate and 2-mercaptoethanol, SDS-PAGE
60000
60800
2 * 60800, calculated from amino acid sequence
62000
65000
65600
-
gel filtration, sucrose density gradient centrifugation, sedimentation equilibrium centrifugation
66000
105200
dynamic light scattering
109600
analytical ultracentrifugation
132000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
monomer
additional information
dimer
-
2 * 31633, sedimentation equilibrium in 6 M guanidine-HCl, sedimentation equilibrium in dodecyl sulfate and 2-mercaptoethanol, SDS-PAGE
homodimer
2 * 60800, calculated from amino acid sequence
homodimer
-
2 * 60800, calculated from amino acid sequence
-
monomer
-
1 * 58500, isozyme PGM1, SDS-PAGE; 1 * 69000, isozyme PGM1, SDS-PAGE
additional information
four-domain architecture, homology modeling, overview
additional information
-
four-domain architecture, homology modeling, overview
-
additional information
-
structure analysis of the active phosphoenzyme, the inactive dephosphoenzyme, and the phosphoenzyme in complex with the substrate analog xylose 1-phosphate, overview
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
additional information
-
phosphoprotein, 1 mol phosphate per mol of enzyme
phosphoprotein
-
phosphorylation of active site Ser108 in wild-type and mutant enzymes
phosphoprotein
-
phosphorylation of conserved catalytic active site residue Ser108 has broad effects on residues in multiple domains. Dephosphorylation of the enzyme may play two critical functional roles: a direct role in the chemical step of phosphoryl transfer and secondly through propagation of structural flexibility. Dephosphorylation has minimal effects on crystal structure of the enzyme
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystallized with vapor diffusion, streak seeding, in ammonium sulfate solution, optimized crystals diffract to 1.5 A resolution
-
crystallization procedure, polyethyleneglycol-400, 1-4.5% must be included in crystal growth medium
-
hanging drop vapor diffusion, 12-15 mg/ml PMM/PGM in 10 mM MOPS, pH 7.0, 1.4 M sodium/potassium tartrate and 100 mM Na-HEPES, pH 7.5, crystals diffract to 1.75 A resolution
-
in complex with inhibitor xylose 1-phosphate or slow substrate ribose 1-phosphate. Both ligands induce an interdomain rearrangement, using different enzyme-ligand interactions
-
phospho- and dephospho-enzyme in complex with reaction intermediate glucose 1,6-bisphosphate at 1.9 and 2.0 A
-
purified recombinant detagged enzyme, hanging drop vapor diffusion and microseeding techniques, 1.3 to 1.4 M sodium/potassium tartrate and 100 mM HEPES, pH 7.5, X-ray diffraction structure determination and analysis at 1.8 A resolution, modeling
-
purified recombinant untagged enzyme mutant H329A, from 1.2-1.6 M Na,K tartrate and 100 mM Na HEPES, pH 7.5, X-ray diffraction structure determination and analysis at 1.8 A resolution, modeling
-
hanging drop vapor diffusion method, using 0.1 M Bis-Tris, pH 6.5, 0.2 M MgCl2, and 25% (w/v) PEG 3350
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 10
-
at pH 7.0 only 17.5% of the relative activity is recovered, the enzyme retains 14% of its initial activity after incubation at pH 10.0
714859
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 60
-
PGM is almost stable (12% loss of the activity) at 30°C for 60 min, while almost complete loss of activity is observed at 50 and 60°C after 10 min
50
52
60 - 70
-
at 60°C PGM is relatively stable and loses 10% of its initial activity after incubation for 8 h. At 70°C, it deactivates quickly with a half-life of 0.8 h. PGM at a concentration of 500 nM has a half-life of 30 h at 60°C, while 2 nM or 50 nM PGM loses nearly 100% of activity within 12 h. Thermostability of PGM at a low concentration (2 nM, 100 units/l) is enhanced by 12fold at 60°C with addition of 1 mg/ml bovine serum albumin, 0.1% (v/v) Triton X-100, 5 mM Mg2+, and 0.5 mM Mn2+
100
50
-
phosphoglucomutase I, 30 min, 50% loss of activity, 80 min, 75% loss of activity; phosphoglucomutase II, 15 min, 50% loss of activity, 80 min, 95% loss of activity
52
-
isozyme PGM1, 10 min, 80% loss of activity; isozyme PGM2, 10 min, 50% loss of activity
52
-
isozyme PGM1, 15 min, 90% loss of activity; isozyme PGM2, 15 min, 55% loss of activity
100
-
highly stable, half-life of about 85 min in boiling water in presence of 10mM Mg2+
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
at pH 7.5, the PGM activity in the HEPES buffer is 20% lower than in the Tris-HCl buffer
-
extremely unstable in crude extracts, protease sensitive, Bacillus subtilis 168 SR 22 can be used as a protease-negative mutant
-
freezing and thawing results in almost total loss of activity, freeze-dried enzyme stable
-
loss of activity is observed when phosphate buffer is used in the pH range of 6.0-8.0
-
stable in 5 mM acetate buffer or 10 mM citrate buffer, pH 5.5, 4 C, but in 5 mM Tris-HCl buffer pH 7.4, 80% loss of activity per day
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, fast-frozen in LN2 and stored for 2 years without affecting the sample homogeneity
-
4-6°C, 0.05 M acetate buffer, pH 5.0, crystalline enzyme form, many months stable
-
4°C, crude enzyme extract, 0.2 mM EDTA, 10% glycerol, pH 6.5, 3-4 weeks stable
-
4°C, purified enzyme, 75% saturated ammonium sulfate, 0.2 mM EDTA, 10% glycerol, pH 6.5, 3 months stable
-
4°C, saturated ammonium sulfate, 0.1 M Na2HPO4-HCl, pH 7.0, 0.1 mM EDTA, 1 mM Mg2+, 3 months stable
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
glutathione Sepharose column chromatography; glutathione Sepharose column chromatography
heat treatment 85°C, 20 min, anion-exchange, hydrophobic and gel filtration column chromatography
-
His-Select Ni-Affinity gel column chromatography, gel filtration
partial
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3), removal of the His-tag, purification by nickel affinity chromatography and dialysis
-
recombinant His-tagged Pgm1, Pgm2, and Pgm3 from Escherichia coli strain BL21 (DE3)
-
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, protein refolding, and ultrafiltration
recombinant PGM
recombinant protein is purified by centrifugation und affinity chromatography with Ni-NTA Superflow cartridge. Purity is assessed by SDS-PAGE
-
recombinant untagged mutant enzyme from Escherichia coli strain BL21(DE3) by ammonium sulfate fractionation, anion exchange and hydrophobic interaction chromatography and dialysis, recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloned and homologously overexpressed in Lactococcus lactis subsp. cremoris strain NZ9000, introducing 6xHis-tag
-
expressed in Eascherichia coli and Saccharomyces cerevisiae BY4741 wild type and pgm1DELTA/pgm2DELTA mutant strain
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells; expressed in Escherichia coli BL21(DE3) cells
expression in Agrobacterium tumefaciens; expression in Agrobacterium tumefaciens; expression in Agrobacterium tumefaciens
expression in Escherichia coli
expression of cytosolic and plastidial isozymes in Nicotiana tabacum cv. Xanthi using the cauliflower mosaic virus 35S promoter. The transgenic plants expressing Arabidopsis plastidial PGM show 3.5-8.2fold higher enzyme activity compared to the wild-type, and leaf starch and sucrose contents increase 2.3-3.2fold and 1.3-1.4fold, respectively over wild-type levels, while transgenic plants expressing Arabidopsis cytosolic PGM show a 2.1-3.4fold increase in PGM activity over wild-type and a decrease of leaf starch content, but no change in sucrose content
-
expression of N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
expression of the His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), expression of untagged mutant H329A in Escherichia coli strain BL21(DE3)
-
gene pgmA, sequence comparison, phylogenetic analysis and expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3) in inclusion bodies
gene pgmG, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, overexpression of the His-tagged enzyme in Escherichia coli strain BL21(DE3), cloning in Escherichia coli strain DH5alpha
genes pgm1, pgm2, and pgm3, cloning in Escherichia coli strain DH5alpha, expression of His-tagged enzymes in Escherichia coli strain BL21 (DE3)
-
overexpression in Escherichia coli
overexpression of histidine-tagged fusion protein in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
high SpgM expression is correlated with the lactams ceftazidime, ticarcillin/clavulanic acid, and piperacillin/tazobactam
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H329A
-
site-directed mutagenesis, crystal structure determination and comparison, the mutant shows no significant changes from the wild-type enzyme, excluding structural disruption as the source of its compromised activity. The kcat of the mutant is 3000fold reduced relative to the wild-type enzyme
N110A
-
no remarkable differences in Km and Vmax value compared to wild-type, but intermediate glucose-1,6-bisphosphate dissociates from mutant 25times more often than from wild-type
R15A
-
no remarkable differences in Km and Vmax value compared to wild-type, but intermediate glucose-1,6-bisphosphate dissociates from mutant 25times more often than from wild-type
R20A
R247A
S101A
S158T
S309A
activity of mutant enzyme with D-glucose 6-phosphate is 58% compared to activity of wild-type enzyme
S309D
activity of mutant enzyme with D-glucose 6-phosphate is 4% compared to activity of wild-type enzyme
S309N
activity of mutant enzyme with D-glucose 6-phosphate is 27% compared to activity of wild-type enzyme
S309Q
activity of mutant enzyme with D-glucose 6-phosphate is 22% compared to activity of wild-type enzyme
S309T
activity of mutant enzyme with D-glucose 6-phosphate is 36% compared to activity of wild-type enzyme
S309V
activity of mutant enzyme with D-glucose 6-phosphate is 36% compared to activity of wild-type enzyme
S309A
-
activity of mutant enzyme with D-glucose 6-phosphate is 58% compared to activity of wild-type enzyme
-
S309N
-
activity of mutant enzyme with D-glucose 6-phosphate is 27% compared to activity of wild-type enzyme
-
S309Q
-
activity of mutant enzyme with D-glucose 6-phosphate is 22% compared to activity of wild-type enzyme
-
S309T
-
activity of mutant enzyme with D-glucose 6-phosphate is 36% compared to activity of wild-type enzyme
-
S309V
-
activity of mutant enzyme with D-glucose 6-phosphate is 36% compared to activity of wild-type enzyme
-
additional information
R247A
-
no remarkable differences in Km and Vmax value compared to wild-type, modest increase in dissociation of intermediate glucose-1,6-bisphosphate from enzyme
S101A
-
mutant protein PH0923S101A to investigate the role of the serine residue
S101A
-
mutant protein PH0923S101A to investigate the role of the serine residue
-
additional information
-
recombinant expression of plastidial phosphoglucomutase in Nicotiana tabacum cv. Xanthi stimulates photosynthetic carbon flow into starch synthesis
additional information
-
overproduction of enzyme leads to increased glycolytic flux and growth rate on galactose. Growth of a conditional knock-out strain is severely impaired when enzyme activity is below the control level
additional information
-
overexpression of phosphoglucomutase gene PGM1 is able to suppress the growth-deficiency of mutant RAS2val19 that is unable to grow on galactose as the sole source of carbon. Elevated levels of enzyme allow for the more efficient utilization of the limiting levels of glucose 1-phosphate that are present in the RASval19 mutant
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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) inclusion bodies
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
food industry
medicine
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inhibition of phosphoglucomutase activity by chronic treatment with Li+ causes compensatory elevation of phosphoglucomutase activity in Li+-treated bipolar patients due to increased expression of PGM1 gene
molecular biology
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phosphoglucomutase is a very suitable marker for analysis of the inter-breed and intra-breed polymorphism for the mulberry silkworm, and for determining the level of genetic variability
drug development
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the activity of the PGM gene of Streptococcus iniae is linked to a variety of structural and functional phenotypes that translate to dramatically decreased virulence in a model of fish meningoencephalitis
drug development
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the activity of the PGM gene of Streptococcus iniae is linked to a variety of structural and functional phenotypes that translate to dramatically decreased virulence in a model of fish meningoencephalitis
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food industry
the enzyme is involved in production of sphingans, extracellular polysaccharides used as thickeners, emulsifiers and gelling agents, its overexpression increases the sphingan production of the transformed cell
food industry
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the enzyme is involved in production of sphingans, extracellular polysaccharides used as thickeners, emulsifiers and gelling agents, its overexpression increases the sphingan production of the transformed cell
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