Information on EC 5.4.2.6 - beta-Phosphoglucomutase

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

EC NUMBER
COMMENTARY
5.4.2.6
-
RECOMMENDED NAME
GeneOntology No.
beta-Phosphoglucomutase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
beta-D-Glucose 1-phosphate = beta-D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
beta-D-Glucose 1-phosphate = beta-D-glucose 6-phosphate
show the reaction diagram
a single Mg2+ coordination site accomodates water, phosphate, and the phosphorane intermediate during catalytic turnover. Bi-bi ping-pong mechanism, substrate induced-fit mechanism allows phosphomutase activity to dominate over the intrinsic phosphatase activity
-
beta-D-Glucose 1-phosphate = beta-D-glucose 6-phosphate
show the reaction diagram
mechanism is a nucleophilic substitution via an associative pathway, enzyme stablizes the phosphorane intermediate along that pathway
-
beta-D-Glucose 1-phosphate = beta-D-glucose 6-phosphate
show the reaction diagram
phosphoryl transfer rather than ligand binding is rate-limiting. Beta-D-glucose 1,6-bisphosphate is a reaction intermediate and binds to the active site in two different orientations with roughly the same efficiency. Reorientation of the beta-D-glucose 1,6-bisphosphate intermediate occurs by diffusion into solvent followed by binding in the opposite orientation
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
group transfer
-
-
intramolecular, phosphate group
-
isomerization
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
galactose degradation I (Leloir pathway)
-
maltose degradation
-
Starch and sucrose metabolism
-
trehalose degradation III
-
trehalose degradation IV
-
SYSTEMATIC NAME
IUBMB Comments
beta-D-Glucose 1,6-phosphomutase
No cofactor requirement has been demonstrated.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
beta-PGM
-
-
-
-
Phosphomutase, beta-glucose
-
-
-
-
TM1254
-
putative beta-phosphoglucomutase
CAS REGISTRY NUMBER
COMMENTARY
68651-99-0
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
var. bacillaris
-
-
Manually annotated by BRENDA team
subsp. lactis, strains 19435 and 65.1
-
-
Manually annotated by BRENDA team
subspecies cremoris IFO 3427
-
-
Manually annotated by BRENDA team
strain MSB8
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
show the reaction diagram
-
7fold lower affinity than with beta-D-glucose
-
r
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
show the reaction diagram
-
-
-
r
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
show the reaction diagram
-
-
-
-
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
show the reaction diagram
-
-
-
-
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
show the reaction diagram
-
-
-
r
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
show the reaction diagram
-
-
-
r
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
show the reaction diagram
-, P71447
-
-
r
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
show the reaction diagram
-
-
-
-
r
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
show the reaction diagram
-
-
-
-
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
show the reaction diagram
-
r
-
-
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
show the reaction diagram
-
r
-
-
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
show the reaction diagram
-
r
-
-
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
show the reaction diagram
-
r
-
-
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
show the reaction diagram
-
r
-
-
beta-D-Glucose 1-phosphate
?
show the reaction diagram
-
the enzyme does not serve solely to degrade maltose, but is also involved in the metabolism of other carbohydrates
-
-
-
beta-D-Glucose 1-phosphate
?
show the reaction diagram
-
enzyme of the nonhydrolytic pathway for maltose metabolism
-
-
-
beta-D-Glucose 1-phosphate
?
show the reaction diagram
-
the enzyme together with a trehalose phosphorylase would constitute a new catabolic pathway for trehalose
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
show the reaction diagram
-
-
-
r
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
show the reaction diagram
-
-
-
r
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
show the reaction diagram
-
-
-
r
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
show the reaction diagram
-, P71447
-
-
r
beta-D-Glucose 1-phosphate
?
show the reaction diagram
-
the enzyme does not serve solely to degrade maltose, but is also involved in the metabolism of other carbohydrates
-
-
-
beta-D-Glucose 1-phosphate
?
show the reaction diagram
-
enzyme of the nonhydrolytic pathway for maltose metabolism
-
-
-
beta-D-Glucose 1-phosphate
?
show the reaction diagram
-
the enzyme together with a trehalose phosphorylase would constitute a new catabolic pathway for trehalose
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Co2+
-
divalent cation, Mg2+, Co2+ or Mn2+ required, maximal activity at 0.4 mM Co2+
Co2+
-
divalent cation required, 1 mM, 37% of the activation relative to Mn2+
Co2+
-
activated by divalent cations at 1 mM in decreasing order: Co2+, Mn2+, Mg2+, Ni2+
Co2+
-
activation at 1 mM, efficiency of activation in descending order, Co2+, Mn2+, Mg2+ and Ni2+
Mg2+
-
divalent cation, Mg2+, Co2+ or Mn2+ required, maximal activity at 1-3 mM Mg2+
Mg2+
-
Mn2+ or Mg2+ required
Mg2+
-
divalent cation required, maximal activation at 1-2 mM
Mg2+
-
activated by divalent cations at 1 mM in decreasing order: Co2+, Mn2+, Mg2+, Ni2+
Mg2+
-
activation at 1 mM, efficiency of activation in descending order, Co2+, Mn2+, Mg2+ and Ni2+
Mg2+
-
required for activity, maximal activity at 10 mM
Mg2+
-
Km-value 0.270 mM
Mg2+
-
required for activity
Mg2+
-
using a Mg2+ ion as a cofactor
Mg2+
-
required
Mn2+
-
divalent cation, Mg2+, Co2+ or Mn2+ required, maximal activity at 0.4 mM Mn2+
Mn2+
-
Mn2+ or Mg2+ required, optimal molar ratio of beta-glucose 1-phosphate to Mn2+ is 5:1
Mn2+
-
divalent cation required, maximal activiation at 0.2-0.5 mM
Mn2+
-
activated by divalent cations at 1 mM in decreasing order: Co2+, Mn2+, Mg2+, Ni2+
Mn2+
-
activation at 1 mM, efficiency of activation in descending order, Co2+, Mn2+, Mg2+ and Ni2+
Ni2+
-
divalent cation required, 1 mM, 9% of the activiation relative to Mn2+
Ni2+
-
activated by divalent cations at 1 mM in decreasing order: Co2+, Mn2+, Mg2+, Ni2+
Ni2+
-
activation at 1 mM, efficiency of activation in descending order, Co2+, Mn2+, Mg2+ and Ni2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
ADP
-
strong inhibition
alpha-D-galactose 1-phosphate
-
competitive
alpha-D-glucose 1-phosphate
-
10 mM, 12% inhibition
ATP
-
strong inhibition
beta-D-glucose-1,6-bisphosphate
-
-
Ca2+
-
0.2 mM Ca2+ in presence of 0.5 mM Mn2+, 21% inhibition
Cd2+
-
0.2 mM Cd2+ in presence of 0.5 mM Mn2+, 92% inhibition
Cd2+
-
strong inhibition
Co2+
-
0.2 mM Co2+ in presence of 0.5 mM Mn2+, 20% inhibition
Cu2+
-
strong inhibition
D-fructose 1-6-diphosphate
-
10 mM, 63% inhibition
D-glucose 6-phosphate
-
10 mM, 11% inhibition
F-
-
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
Fe2+
-
0.2 mM Fe2+ in presence of 0.5 mM Mn2+, 17% inhibition
-
Fe2+
-
1 mM FeCl2, 68% inhibition
-
Hg2+
-
strong inhibition
KF
-
10 mM: 75% inhibition, 17 mM: 100% inhibition
Ni2+
-
0.2 mM Ni2+ in presence of 0.5 mM Mn2+, 29% inhibition
phosphate
-
10 mM, 20% inhibition
Zn2+
-
0.2 mM Zn2+ in presence of 0.5 mM Mn2+, 50% inhibition
Zn2+
-
strong inhibition
magnesium fluoride
-
time-dependent inhibition
additional information
-
no inhibition by NEM and 5,5'-dithiobis(2-nitrobenzoate)
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
arsenate
-
increasemM s activity
arsenate
-
increasemM s activity
beta-D-glucose 1,6-bisphosphate
-
-
beta-D-glucose 1,6-bisphosphate
-
required, Km value 0.0065 mM. Beta-D-glucose 1,6-bisphosphate is a reaction intermediate
beta-D-Glucose 1,6-diphosphate
-
required
beta-D-Glucose 1,6-diphosphate
-
Km: 0.0005 mM; required
beta-D-Glucose 1,6-diphosphate
-
Km: 0.0008; required
beta-D-Glucose 1,6-diphosphate
-
required
D-glucose-1,6-bisphosphate
-
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.021
-
alpha-D-glucose 1-phosphate
-
1-phosphate phosphodismutase activity
0.027
-
alpha-D-glucose 1-phosphate
-
phosphoglucomutase activity
0.004
-
beta-D-glucose 1-phosphate
-
phosphoglucomutase activity
0.0045
-
beta-D-glucose 1-phosphate
-
in the presence of beta-D-glucose 1,6-diphosphate and Mg2+
0.006
-
beta-D-glucose 1-phosphate
-
1-phosphate phosphodismutase activity
0.0078
-
beta-D-glucose 1-phosphate
-
mutant D170A, 25C, pH 7.0
0.0146
-
beta-D-glucose 1-phosphate
-
wild-type, 25C, pH 7.0
0.0147
-
beta-D-glucose 1-phosphate
-
in 50 mM buffer (HEPES, pH 7.2), with 2 mM MgCl2
0.049
-
beta-D-glucose 1-phosphate
-
pH 7.0, 25C
0.39
-
beta-D-glucose 1-phosphate
-
mutant E169A/D170A, 25C, pH 7.0
0.012
-
glucose 1-phosphate
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0012
-
beta-D-glucose 1-phosphate
-
mutant E169A/D170A, 25C, pH 7.0
0.00384
-
beta-D-glucose 1-phosphate
-
mutant D170A, 25C, pH 7.0
17
-
beta-D-glucose 1-phosphate
-
in the presence of beta-D-glucose 1,6-diphosphate and Mg2+
17.1
-
beta-D-glucose 1-phosphate
-
wild-type, 25C, pH 7.0
64.7
-
beta-D-glucose 1-phosphate
-
in 50 mM buffer (HEPES, pH 7.2), with 2 mM MgCl2
177
-
beta-D-glucose 1-phosphate
-
pH 7.0, 25C
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.03
-
alpha-D-galactose 1-phosphate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.463
-
-
-
18
-
-
native beta-PGM
40
-
-
recombinant beta-PGM
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
8
-
pH 6: about 30% of maximal activity, pH 8.0: about 50% of maximal activity
6
8.2
-
6.0: about 35% of maximal activity, pH 8.2: about 15% of maximal activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
50
-
25C: about 70% of maximal activity, 50C: about 40% of maximal activity
PDB
SCOP
CATH
ORGANISM
Bacillus subtilis (strain 168)
Clostridium difficile (strain 630)
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)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25210
-
-
calculation from nucleotide sequence
27000
-
-
gel filtration
29000
-
-
gel filtration
80000
-
-
nonreducing SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 24208, ESI-MS
monomer
-
1 * 25000, SDS-PAGE
monomer
-
x * 25000, SDS-PAGE
monomer
-
1 * 25000, SDS-PAGE
monomer
-
gel filtration
trimer
-
3 * 26500, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phosphoprotein
-
catalysis of reaction proceeds via a phosphoenzyme form
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-
both in complex with inhibitor alpha-D-galactose 1-phosphate or substrate beta-D-glucose 1-phosphate
-
characterization of the solution structure of the MgF3- complex bound to the enzyme active site
-
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
-
in complex with Mg2+
-
sitting drop vapor diffusion method, using 0.1 M trisodium citrate pH 5.0 containing 1.8 M ammonium sulfate
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
9.5
-
30C, 30 min, stable
6
-
-
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
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
-
-
overnight at room temperature, 50% loss of activity
30
-
-
30 min, pH 5.0-9.5
45
-
-
pH 7.0, 15 min, stable up to
45
-
-
no loss of activity
50
-
-
15 min, 12% loss of activity
60
-
-
15 min, 60% loss of activity
95
-
-
no loss of activity after 30 min
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
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
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-70C, 0.02 M phosphate buffer, pH 7.0, stable for at least 6 months
-
-80C, partially purified enzyme, stable for at least 3 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant PgcM
-
QAE-Sephadex A-50, Phenyl-Sepharose, hydroxylapatite, Bio-Gel A-1.5m
-
recombinant native and selenomethionyl beta-PGM
-
recombinant seleno-methionine beta-PGM
-
Toyopearl SuperQ-650M column chromatography, Resource Q column chromatography, and Superdex 75 gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
overexpression in Bacillus mergaterium
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expression of seleno-methionine beta-PGM in Escherichia coli
-
overexpression of native and selenomethionyl beta-PGM in escherichia coli
-
expressed in Escherichia coli Rosetta (DE3) cells
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D170A
-
700fold reduction of kcat-value
D8A
-
no catalytic activity
D8E
-
no catalytic activity
E169A/D170A
-
1400fold reduction of kcat-value
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
analysis
-
a specific method for the quantitative determination of beta-glucose 1-phosphate