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Information on EC 5.4.2.2 - phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent) and Organism(s) Pseudomonas aeruginosa and UniProt Accession P26276
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5.4.2.2 phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent)IUBMB Comments
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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Word Map
- 5.4.2.2
- starch
- hexokinase
- glycogen
- malate
- phosphorylase
- 6-phosphogluconate
-
pyrophosphorylase
- 1-phosphate
- adenylate
- esterase
- erythrocyte
- galactose
- glucose-1-phosphate
- aldolase
-
phosphofructokinase
- transferrin
- gpi
-
allozyme
- haptoglobin
-
malic
-
glucosephosphate
-
zymodemes
- histolytica
-
hardy-weinberg
- entamoeba
- glyoxalase
- adp-glucose
- phosphoglucoisomerase
- glucose-6-phosphatase
-
monomorphic
- plastidial
-
glycogenolysis
- fructokinase
- diptera
- galactose-1-phosphate
-
phosphohexose
-
starch-gel
-
uridylyltransferase
-
5.3.1.9
-
glc-6-p
-
bloodstain
- udp-galactose
-
leloir
- amyloplasts
-
duffy
- udp-glc
- phosphoenzyme
-
isoenzymatic
-
2.7.1.1
- 1,6-diphosphate
- drug development
- molecular biology
- food industry
- medicine
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
phosphoglucomutase, phosphoglucomutase 1, phosphomannomutase/phosphoglucomutase, pmm/pgm, alpha-phosphoglucomutase, pgm/pmm, alpha-pgm, phosphoglucose mutase, phosphoglucomutase1, plastidic phosphoglucomutase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Glucose phosphomutase
-
-
-
-
PGM
-
-
-
-
PGM1
-
-
-
-
PGM2
-
-
-
-
Phosphoglucose mutase
-
-
-
-
Phosphomutase, glucose
-
-
-
-
PMM/PGM
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
isomerization
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
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).
CAS REGISTRY NUMBER
COMMENTARY
9001-81-4
-
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 1-phosphate
alpha-D-glucose 6-phosphate
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 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-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
-
-
r
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
-
-
?
NATURAL SUBSTRATE
NATURAL 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 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
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Disperse Blue 56
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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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Michaelis-Menten steady-state kinetics of wild-type and mutant H329A enzymes, overview
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0.03
alpha-D-glucose 1-phosphate
-
mutant H329A, pH 7.5, temperature not specified in the publication
0.08
alpha-D-glucose 1-phosphate
-
wild-type enzyme, pH 7.5, temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.03
alpha-D-glucose 1-phosphate
-
mutant H329A, pH 7.5, temperature not specified in the publication
95
alpha-D-glucose 1-phosphate
-
wild-type enzyme, pH 7.5, temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1
alpha-D-glucose 1-phosphate
-
mutant H329A, pH 7.5, temperature not specified in the publication
1188
alpha-D-glucose 1-phosphate
-
wild-type enzyme, pH 7.5, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
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the enzyme belongs to the alpha-D-phosphohexomutase enzyme superfamily
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
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
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
structure analysis of the active phosphoenzyme, the inactive dephosphoenzyme, and the phosphoenzyme in complex with the substrate analog xylose 1-phosphate, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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in complex with inhibitor xylose 1-phosphate or slow substrate ribose 1-phosphate. Both ligands induce an interdomain rearrangement, using different enzyme-ligand interactions
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phospho- and dephospho-enzyme in complex with reaction intermediate glucose 1,6-bisphosphate at 1.9 and 2.0 A
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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
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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
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PROTEIN VARIANTS
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
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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3), removal of the His-tag, purification by nickel affinity chromatography and dialysis
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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
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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)
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ye, R.W.; Zielinski, N.A.; Chakrabarty, A.M.
Purification and characterization of phosphomannomutase/phosphoglucomutase from Pseudomonas aeruginosa involved in biosynthesis of both alginate and lipopolysaccharide
J. Bacteriol.
176
4851-4877
1994
Pseudomonas aeruginosa
Regni, C.A.; Tipton, P.A.; Beamer, L.J.
Crystallization and initial crystallographic analysis of phosphomannomutase/phosphoglucomutase from Pseudomonas aeruginosa
Acta Crystallogr. Sect. D
56
761-762
2000
Pseudomonas aeruginosa
Naught, L.E.; Tipton, P.A.
Kinetic mechanism and pH dependence of the kinetic parameters of Pseudomonas aeruginosa phosphomannomutase/phosphoglucomutase
Arch. Biochem. Biophys.
396
111-118
2001
Pseudomonas aeruginosa
Naught, L.E.; Regni, C.; Beamer, L.J.; Tipton, P.A.
Roles of active site residues in Pseudomonas aeruginosa phosphomannomutase/phosphoglucomutase
Biochemistry
42
9946-9951
2003
Pseudomonas aeruginosa (P26276), Pseudomonas aeruginosa
Liu, H.Y.; Wang, Z.; Regni, C.; Zou, X.; Tipton, P.A.
Detailed kinetic studies of an aggregating inhibitor; inhibition of phosphomannomutase/phosphoglucomutase by disperse blue 56
Biochemistry
43
8662-8669
2004
Pseudomonas aeruginosa
Regni, C.; Shackelford, G.S.; Beamer, L.J.
Complexes of the enzyme phosphomannomutase/phosphoglucomutase with a slow substrate and an inhibitor
Acta Crystallogr. Sect. F
F62
722-726
2006
Pseudomonas aeruginosa
Regni, C.; Schramm, A.M.; Beamer, L.J.
The reaction of phosphohexomutase from Pseudomonas aeruginosa: structural insights into a simple processive enzyme
J. Biol. Chem.
281
15564-15571
2006
Pseudomonas aeruginosa
Lee, Y.; Mehra-Chaudhary, R.; Furdui, C.; Beamer, L.J.
Identification of an essential active-site residue in the alpha-D-phosphohexomutase enzyme superfamily
FEBS J.
280
2622-2632
2013
Pseudomonas aeruginosa
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