Information on EC 5.4.2.6 - beta-Phosphoglucomutase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
5.4.2.6
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RECOMMENDED NAME
GeneOntology No.
beta-Phosphoglucomutase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
beta-D-Glucose 1-phosphate = beta-D-glucose 6-phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
group transfer
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intramolecular, phosphate group
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isomerization
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
degradation of hexoses
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kojibiose degradation
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maltose degradation
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Starch and sucrose metabolism
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trehalose degradation III
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trehalose degradation IV
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SYSTEMATIC NAME
IUBMB Comments
beta-D-Glucose 1,6-phosphomutase
The enzyme requires Mg2+ and phosphorylation of an aspartate residue at the active site. The enzyme is able to autophosphorylate itself with its substrate beta-D-glucose 1-phosphate. Although this is a slow reaction, only a single turnover is required for activation. Once the phosphorylated enzyme is formed, it generates the reaction intermediate beta-D-glucose 1,6-bisphosphate, which can be used to phosphorylate the enzyme in subsequent cycles [4]. cf. EC 5.4.2.2, phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent).
CAS REGISTRY NUMBER
COMMENTARY hide
68651-99-0
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
gene SMU.1747c or pgmB
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Manually annotated by BRENDA team
gene SMU.1747c or pgmB
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Manually annotated by BRENDA team
strain MSB8
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
show the reaction diagram
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7fold lower affinity than with beta-D-glucose
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r
beta-D-Glucose 1-phosphate
?
show the reaction diagram
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
beta-D-Glucose 1-phosphate
?
show the reaction diagram
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
alpha-D-galactose 1-phosphate
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competitive
alpha-D-glucose 1-phosphate
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10 mM, 12% inhibition
beta-D-glucose-1,6-bisphosphate
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-
Ca2+
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0.2 mM Ca2+ in presence of 0.5 mM Mn2+, 21% inhibition
CaCl2
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1 mM, 77% inhibition
Co2+
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0.2 mM Co2+ in presence of 0.5 mM Mn2+, 20% inhibition
D-fructose 1-6-diphosphate
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10 mM, 63% inhibition
D-glucose 6-phosphate
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10 mM, 11% inhibition
F-
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formation of a MgF3- transition state analogue when glucose 6-phosphate, magnesium, and fluoride are present with the enzyme, in which MgF3- mimics the transferring PO3- moiety
fluoride
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KF
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10 mM: 75% inhibition, 17 mM: 100% inhibition
magnesium fluoride
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time-dependent inhibition
Ni2+
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0.2 mM Ni2+ in presence of 0.5 mM Mn2+, 29% inhibition
phosphate
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10 mM, 20% inhibition
additional information
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no inhibition by NEM and 5,5'-dithiobis(2-nitrobenzoate)
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
arsenate
beta-D-glucose 1,6-bisphosphate
beta-D-Glucose 1,6-diphosphate
D-glucose-1,6-bisphosphate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.021 - 0.027
alpha-D-glucose 1-phosphate
0.004 - 2.08
beta-D-glucose 1-phosphate
0.012
glucose 1-phosphate
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0012 - 177
beta-D-glucose 1-phosphate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9.07
beta-D-glucose 1-phosphate
Pyrococcus sp.
I3RFR5
90C, pH not specified in the publication; pH 6.0, 90C
725
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03
alpha-D-galactose 1-phosphate
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.51
90C, pH not specified in the publication, conversion of beta-D-glucose 6-phosphate into beta-D-glucose 1-phosphate; pH 6.0, 90C, conversion from beta-D-glucose 6-phosphate to beta-D-glucose 1-phosphate
18
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native beta-PGM
40
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recombinant beta-PGM
46.81
90C, pH not specified in the publication, conversion of beta-D-glucose 1-phosphate into beta-D-glucose 6-phosphate; pH 6.0, 90C, conversion from beta-D-glucose 1-phosphate to beta-D-glucose 6-phosphate
additional information
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9.5
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6 - 8.2
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6.0: about 35% of maximal activity, pH 8.2: about 15% of maximal activity
6 - 8
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pH 6: about 30% of maximal activity, pH 8.0: about 50% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 50
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25C: about 70% of maximal activity, 50C: about 40% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus subtilis (strain 168)
Escherichia coli (strain K12)
Lactococcus lactis subsp. lactis (strain IL1403)
Lactococcus lactis subsp. lactis (strain IL1403)
Lactococcus lactis subsp. lactis (strain IL1403)
Lactococcus lactis subsp. lactis (strain IL1403)
Lactococcus lactis subsp. lactis (strain IL1403)
Lactococcus lactis subsp. lactis (strain IL1403)
Lactococcus lactis subsp. lactis (strain IL1403)
Lactococcus lactis subsp. lactis (strain IL1403)
Lactococcus lactis subsp. lactis (strain IL1403)
Lactococcus lactis subsp. lactis (strain IL1403)
Lactococcus lactis subsp. lactis (strain IL1403)
Lactococcus lactis subsp. lactis (strain IL1403)
Lactococcus lactis subsp. lactis (strain IL1403)
Lactococcus lactis subsp. lactis (strain IL1403)
Lactococcus lactis subsp. lactis (strain IL1403)
Lactococcus lactis subsp. lactis (strain IL1403)
Lactococcus lactis subsp. lactis (strain IL1403)
Lactococcus lactis subsp. lactis (strain IL1403)
Peptoclostridium difficile (strain 630)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25210
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calculation from nucleotide sequence
27000
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gel filtration
29000
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gel filtration
80000
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nonreducing SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
trimer
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3 * 26500, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
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catalysis of reaction proceeds via a phosphoenzyme form
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
beta-PGM is transferred to 1 mM HEPES, pH 7.5, 10 mM MgCl2 and 0.1 mM dithiothreitol, final beta-PGM concentration at 15 mg/ml, crystals are obtained from either 150 mM ammonium acetate, 100 mM trisodium citrate dihydrate, pH 4.5, 25% polyethylene glycol 4000 or 100 mM ammonium fluoride, 16% polyethylene glycol 3350 by hanging-drop vapor diffusion, crystals of selenium methionyl-substituted beta-PGM diffract to 2.3 A
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both in complex with inhibitor alpha-D-galactose 1-phosphate or substrate beta-D-glucose 1-phosphate
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characterization of the solution structure of the MgF3- complex bound to the enzyme active site
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crystals of phosphorylated native beta-PGM are grown at pH 7.5 in the presence of 5 M Mg2+ using the vapor-diffusion method with hanging drop geometry, 100 mM ammonium fluoride and 16% polyethylene glycol 3350 are used as precipitating agents, crystals diffrakt to 2.3 A
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in complex with Mg2+
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purified recombinant enzyme in complex with transition-state analogue fluoromagnesate and glucose 6-phosphate or ground-state analogue fluoroaluminate and glucose 6-phosphate, sitting drop vapour diffusion method, mixing of 15 mg/mL 50 mM K+ HEPES, pH 7.2, 5 mM MgCl2, 1 mM azide, 0.1 mM DTT, 10 mM NH4F, and 10 mM BeCl2 1:1 with the precipitant containing 26-30% w/v PEG 4000, 200 mM Na acetate, and 100 mM Tris, pH 7.5, X-ray diffraction structure determination and analysis at 1.65 A resolution, molecular replacement
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sitting drop vapor diffusion method, using 0.1 M trisodium citrate pH 5.0 containing 1.8 M ammonium sulfate
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9.5
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30C, 30 min, stable
3338
6
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0C: about 70% loss of activity after 2 days, -20C: about 30% loss of activity after 2 days, -70C: no loss of activity after 2 days
3333
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
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overnight at room temperature, 50% loss of activity
50
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15 min, 12% loss of activity
60
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15 min, 60% loss of activity
70
20 min, stable
95
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no loss of activity after 30 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
after 12 h in 0.02 M imidazole buffer, at pH 7.0, totally inactivated both at 0C and at -20C. Glycylglycine, N-2-hydroxyethylpiperazine-N'-2-ethanesulfonic acid and phosphate at the same conditions are able to preserve most of the enzyme activity. Cacodylate, ethylmorpholidate, Tris-maleate and glycerophosphate have an intermediate action
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70C, 0.02 M phosphate buffer, pH 7.0, stable for at least 6 months
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-80C, partially purified enzyme, stable for at least 3 months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; recombinant enzyme
partial
QAE-Sephadex A-50, Phenyl-Sepharose, hydroxylapatite, Bio-Gel A-1.5m
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recombinant native and selenomethionyl beta-PGM
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recombinant PgcM
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recombinant seleno-methionine beta-PGM
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Toyopearl SuperQ-650M column chromatography, Resource Q column chromatography, and Superdex 75 gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli Rosetta (DE3) cells
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expression in Escherichia coli
expression in Escherichia coli; heterologous expression in Escherichia coli
expression of seleno-methionine beta-PGM in Escherichia coli
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gene SMU.1747c or pgmB, DNA and amino acid sequence determination and analysis, genetic organization
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overexpression in Bacillus mergaterium
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overexpression of native and selenomethionyl beta-PGM in escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D170A
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700fold reduction of kcat-value
D8A
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no catalytic activity
D8E
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no catalytic activity
E169A/D170A
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1400fold reduction of kcat-value
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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a specific method for the quantitative determination of beta-glucose 1-phosphate
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