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Information on EC 5.4.2.6 - beta-Phosphoglucomutase
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5.4.2.6 beta-PhosphoglucomutaseIUBMB Comments
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 . cf. EC 5.4.2.2, phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent).
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Word Map
- 5.4.2.6
- 1-phosphate
- lactis
- maltose
-
phosphorane
-
dehalogenase
- trehalose
- 1,6-bisphosphate
-
haloacid
-
lactococci
- alpha-glucose
- analysis
The enzyme appears in viruses and cellular organisms
Synonyms
beta-phosphoglucomutase, beta-pgm, betapgm, tm1254, pspgm, py04_1503, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
beta-PGM
beta-phosphoglucomutase
betaPGM
Phosphomutase, beta-glucose
-
-
-
-
PsPGM
Py04_1503
TM1254
YcjU
beta-PGM
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
beta-D-Glucose 1-phosphate = beta-D-glucose 6-phosphate
-
-
-
-
beta-D-Glucose 1-phosphate = beta-D-glucose 6-phosphate
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
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
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
-
beta-D-Glucose 1-phosphate = beta-D-glucose 6-phosphate
reaction mechanism of the phosphoryl transfer starting from the bisphosphate intermediate beta-D-glucose-1,6-(bis)phosphate in both directions of the reversible reaction, overview. The calculated energy barrier of the reaction for the beta-D-glucose 1-phosphate to beta-D-glucose 1,6-diphosphate step is only slightly higher than for the beta-G1,6diP to beta-G6P step. Residues Ser114 and Lys145 and Mg2+ play important roles in stabilizing the large negative charge on the phosphate through strong coordination with the phosphate oxygens and guiding the phosphate group throughout the catalytic process
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
group transfer
-
-
intramolecular, phosphate group
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isomerization
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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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).
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CAS REGISTRY NUMBER
COMMENTARY
68651-99-0
-
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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 1-phosphate
alpha-D-glucose 6-phosphate
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7fold lower affinity than with beta-D-glucose
-
r
beta-D-Glucose 1-phosphate
?
-
the enzyme together with a trehalose phosphorylase would constitute a new catabolic pathway for trehalose
-
-
?
beta-D-Glucose 1-phosphate
?
-
the enzyme does not serve solely to degrade maltose, but is also involved in the metabolism of other carbohydrates
-
-
?
beta-D-Glucose 1-phosphate
?
-
enzyme of the nonhydrolytic pathway for maltose metabolism
-
-
?
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
the enzyme exhibits less than 1% of the catalytic activity (relative to beta-D-glucose-1-phosphate) with alpha-D-glucose-1-phosphate
-
-
r
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
the enzyme exhibits less than 1% of the catalytic activity (relative to beta-D-glucose-1-phosphate) with alpha-D-glucose-1-phosphate
-
-
r
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
-
-
-
?
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
-
-
-
-
?
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
-
r
-
?
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
-
r
-
?
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
-
-
-
-
r
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
-
via stabile intermediate beta-D-glucose-1,6-(bis)phosphate
-
-
r
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
-
-
-
?
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
the enzyme is involved in conversion of kojibiose into beta-D-glucose 6-phosphate, a substrate of the glycolytic pathway. Disaccharide utilization pathway via phosphorolysis in hyperthermophilic archaea
-
-
r
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
the enzyme is involved in the kojibiose catabolic pathway
-
-
r
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
conversion activity from beta-D-glucose 1-phosphate to beta-D-glucose 6-phosphate is 46.81 U/mg, and reverse conversion activity from beta-D-glucose 6-phosphate to beta-D-glucose 1-phosphate is 3.51 U/mg
-
-
r
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
the enzyme is involved in conversion of kojibiose into beta-D-glucose 6-phosphate, a substrate of the glycolytic pathway. Disaccharide utilization pathway via phosphorolysis in hyperthermophilic archaea
-
-
r
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
the enzyme is involved in the kojibiose catabolic pathway
-
-
r
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
conversion activity from beta-D-glucose 1-phosphate to beta-D-glucose 6-phosphate is 46.81 U/mg, and reverse conversion activity from beta-D-glucose 6-phosphate to beta-D-glucose 1-phosphate is 3.51 U/mg
-
-
r
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
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-
-
-
?
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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
beta-D-Glucose 1-phosphate
?
-
the enzyme together with a trehalose phosphorylase would constitute a new catabolic pathway for trehalose
-
-
?
beta-D-Glucose 1-phosphate
?
-
the enzyme does not serve solely to degrade maltose, but is also involved in the metabolism of other carbohydrates
-
-
?
beta-D-Glucose 1-phosphate
?
-
enzyme of the nonhydrolytic pathway for maltose metabolism
-
-
?
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
-
-
-
?
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
the enzyme is involved in conversion of kojibiose into beta-D-glucose 6-phosphate, a substrate of the glycolytic pathway. Disaccharide utilization pathway via phosphorolysis in hyperthermophilic archaea
-
-
r
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
the enzyme is involved in the kojibiose catabolic pathway
-
-
r
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
the enzyme is involved in conversion of kojibiose into beta-D-glucose 6-phosphate, a substrate of the glycolytic pathway. Disaccharide utilization pathway via phosphorolysis in hyperthermophilic archaea
-
-
r
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
the enzyme is involved in the kojibiose catabolic pathway
-
-
r
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Mg2+
Mn2+
Ni2+
Co2+
-
divalent cation, Mg2+, Co2+ or Mn2+ required, maximal activity at 0.4 mM Co2+
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+
Co2+
-
divalent cation required, 1 mM, 37% of the activation relative to Mn2+
Mg2+
activation constant is 0.135 mM. In the absence of added Mg2+, the observed catalytic activity is less than 2% of the turnover observed in the presence of 2.0 mM Mg2+
Mg2+
-
divalent cation, Mg2+, Co2+ or Mn2+ required, maximal activity at 1-3 mM Mg2+
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+
conversion of beta-D-glucose 1-phosphate into beta-D-glucose 6-phosphate in the presence of 6 mM MgCl2
Mn2+
-
divalent cation, Mg2+, Co2+ or Mn2+ required, maximal activity at 0.4 mM Mn2+
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+
Mn2+
-
Mn2+ or Mg2+ required, optimal molar ratio of beta-glucose 1-phosphate to Mn2+ is 5:1
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+
Ni2+
-
divalent cation required, 1 mM, 9% of the activiation relative to Mn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
beta-D-glucose 1-phosphate
substrate inhibition is observed at concentrations of beta-D-glucose-1-phosphate greater than 0.2 mM
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
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
LITERATURE
IMAGE
beta-D-glucose 1,6-bisphosphate
-
required, Km value 0.0065 mM. Beta-D-glucose 1,6-bisphosphate is a reaction intermediate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0045
beta-D-glucose 1-phosphate
-
in the presence of beta-D-glucose 1,6-diphosphate and Mg2+
0.0147
beta-D-glucose 1-phosphate
-
in 50 mM buffer (HEPES, pH 7.2), with 2 mM MgCl2
2.08
beta-D-glucose 1-phosphate
90°C, pH not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
17
beta-D-glucose 1-phosphate
-
in the presence of beta-D-glucose 1,6-diphosphate and Mg2+
64.7
beta-D-glucose 1-phosphate
-
in 50 mM buffer (HEPES, pH 7.2), with 2 mM MgCl2
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
9.07
beta-D-glucose 1-phosphate
90°C, pH not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
113
3.51
46.81
3.51
90°C, pH not specified in the publication, conversion of beta-D-glucose 6-phosphate into beta-D-glucose 1-phosphate
3.51
pH 6.0, 90°C, conversion from beta-D-glucose 6-phosphate to beta-D-glucose 1-phosphate
46.81
90°C, pH not specified in the publication, conversion of beta-D-glucose 1-phosphate into beta-D-glucose 6-phosphate
46.81
pH 6.0, 90°C, conversion from beta-D-glucose 1-phosphate to beta-D-glucose 6-phosphate
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
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