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
5.4.2.6
-
RECOMMENDED NAME
GeneOntology No.
beta-Phosphoglucomutase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
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
-
beta-D-Glucose 1-phosphate = beta-D-glucose 6-phosphate
show the reaction diagram
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
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
group transfer
-
-
intramolecular, phosphate group
-
isomerization
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
degradation of hexoses
-
-
galactose degradation I (Leloir pathway)
-
-
kojibiose degradation
-
-
maltose degradation
-
-
Starch and sucrose metabolism
-
-
trehalose degradation III
-
-
trehalose degradation IV
-
-
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).
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
beta-PGM
-
-
-
-
beta-phosphoglucomutase
I3RFR5
-
beta-phosphoglucomutase
I3RFR5
-
-
Phosphomutase, beta-glucose
-
-
-
-
PsPGM
I3RFR5
-
PsPGM
I3RFR5
-
-
Py04_1503
I3RFR5
locus name
Py04_1503
I3RFR5
locus name
-
TM1254
-
putative beta-phosphoglucomutase
CAS REGISTRY NUMBER
COMMENTARY
68651-99-0
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
deletion of pgmB affects known virulence factors of Streptococcus mutans, specifically acid tolerance, mutant strain MU1593 is defective in its acid-responsiveness. The DELTApgmB strain shows a decreased ability to survive acid challenge. Additionally, the strain lacking beta-phosphoglucomutase has a diminished glycolytic profile compared with the parental strain. Proton permeability is increased in strain MU1593. Deletion of pgmB has a negative impact on the virulence of Streptococcus mutans in the Galleria mellonella (greater wax worm) animal model. Phenotype of strain MU1593, overview
physiological function
I3RFR5
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, the enzyme is involved in the kojibiose catabolic pathway
physiological function
-
the enzyme is involved in the kojibiose catabolic pathway
physiological function
-
The enzyme plays a role at the juncture of carbohydrate metabolism and virulence. beta-Phosphoglucomutase contributes to aciduricity in Streptococcus mutans
physiological function
-
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, the enzyme is involved in the kojibiose catabolic pathway
-
physiological function
-
The enzyme plays a role at the juncture of carbohydrate metabolism and virulence. beta-Phosphoglucomutase contributes to aciduricity in Streptococcus mutans
-
malfunction
-
deletion of pgmB affects known virulence factors of Streptococcus mutans, specifically acid tolerance, mutant strain MU1593 is defective in its acid-responsiveness. The DELTApgmB strain shows a decreased ability to survive acid challenge. Additionally, the strain lacking beta-phosphoglucomutase has a diminished glycolytic profile compared with the parental strain. Proton permeability is increased in strain MU1593. Deletion of pgmB has a negative impact on the virulence of Streptococcus mutans in the Galleria mellonella (greater wax worm) animal model. Phenotype of strain MU1593, overview
-
additional information
-
fluoromagnesate and fluoroaluminate complexes of beta-phosphoglucomutase demonstrate the importance of charge balance in transition-state stabilization for phosphoryl transfer enzymes, overview
additional information
-
reaction mechanism analysis by docking techniques and QM/MM theoretical method, overview. 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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
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
I3RFR5
-
-
-
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
beta-D-Glucose 6-phosphate
show the reaction diagram
-
r
-
-
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
show the reaction diagram
I3RFR5
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, the enzyme is involved in the kojibiose catabolic pathway
-
-
r
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
show the reaction diagram
-
the enzyme is involved in the kojibiose catabolic pathway
-
-
r
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
show the reaction diagram
I3RFR5
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
show the reaction diagram
-
via stabile intermediate beta-D-glucose-1,6-(bis)phosphate
-
-
r
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
show the reaction diagram
I3RFR5
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, the enzyme is involved in the kojibiose catabolic pathway, 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
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
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
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
I3RFR5
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, the enzyme is involved in the kojibiose catabolic pathway
-
-
r
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
show the reaction diagram
-
the enzyme is involved in the kojibiose catabolic pathway
-
-
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
-
-
-
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
show the reaction diagram
I3RFR5
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, the enzyme is involved in the kojibiose catabolic pathway
-
-
r
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
show the reaction diagram
-
-
-
-
r
METALS and IONS
ORGANISM
UNIPROT
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
Mg2+
I3RFR5
conversion of beta-D-glucose 1-phosphate into beta-D-glucose 6-phosphate in the presence of 6 mM MgCl2; no activity without Mg2+. 6 mM is the optimal concentration
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
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
CaCl2
-
1 mM, 77% 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
fluoride
-
-
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
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]
SUBSTRATE
ORGANISM
UNIPROT
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
2.08
beta-D-glucose 1-phosphate
I3RFR5
90C, pH not specified in the publication; pH 6.0, 90C
0.012
glucose 1-phosphate
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
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
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
9.07
beta-D-glucose 1-phosphate
I3RFR5
90C, pH not specified in the publication; pH 6.0, 90C
725
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.03
alpha-D-galactose 1-phosphate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.51
I3RFR5
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
-
native beta-PGM
40
-
recombinant beta-PGM
46.81
I3RFR5
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
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 9
I3RFR5
-
5 - 9.5
-
-
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
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
95
I3RFR5
-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 50
-
25C: about 70% of maximal activity, 50C: about 40% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
no difference in growth rate between wild-type strain UA159 and enzyme deletion mutant MU1593 during the exponential growth phase in medium buffered to pH 7.0
Manually annotated by BRENDA team
additional information
-
no difference in growth rate between wild-type strain UA159 and enzyme deletion mutant MU1593 during the exponential growth phase in medium buffered to pH 7.0
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
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
LITERATURE
25210
-
calculation from nucleotide sequence
3336
27000
-
gel filtration
3333
28000
-
gel filtration
3337
29000
-
gel filtration
3335
80000
-
nonreducing SDS-PAGE
641630
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
I3RFR5
x * 25000, SDS-PAGE
?
-
x * 24208, ESI-MS
?
-
x * 24500, about, sequence calculation
?
-
x * 25000, SDS-PAGE
-
?
-
x * 24500, about, sequence calculation
-
monomer
-
1 * 25000, SDS-PAGE
monomer
-
1 * 25000, SDS-PAGE
monomer
-
x * 25000, SDS-PAGE
monomer
-
gel filtration
trimer
-
3 * 26500, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
-
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
-
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+
-
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
-
sitting drop vapor diffusion method, using 0.1 M trisodium citrate pH 5.0 containing 1.8 M ammonium sulfate
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 9.5
-
30C, 30 min, stable
3338
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
3333
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
-
overnight at room temperature, 50% loss of activity
3337
30
-
30 min, pH 5.0-9.5
3338
37
-
stable for 1 week
3338
45
-
pH 7.0, 15 min, stable up to
3338
45
-
no loss of activity
3338
50
-
15 min, 12% loss of activity
3338
60
-
15 min, 60% loss of activity
3338
70
I3RFR5
20 min, stable
725294
95
-
no loss of activity after 30 min
641630
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
-
STORAGE STABILITY
ORGANISM
UNIPROT
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
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
-
; recombinant enzyme
I3RFR5
Toyopearl SuperQ-650M column chromatography, Resource Q column chromatography, and Superdex 75 gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
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
-
expression in Escherichia coli; heterologous expression in Escherichia coli
I3RFR5
gene SMU.1747c or pgmB, DNA and amino acid sequence determination and analysis, genetic organization
-
expressed in Escherichia coli Rosetta (DE3) cells
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D170A
-
700fold reduction of kcat-value
D8A
-
no catalytic activity
D8E
-
no catalytic activity
E169A/D170A
-
1400fold reduction of kcat-value
additional information
-
generation and genetic complementation of the pgmB deletion MU1593 mutant strain, the mutant strain is acid-sensitive and exhibits reduced glycolytic output from glucose challenge. The fatty acid profile of MU1593 is altered compared with wild-type UA159 in all growth conditions tested
additional information
-
generation and genetic complementation of the pgmB deletion MU1593 mutant strain, the mutant strain is acid-sensitive and exhibits reduced glycolytic output from glucose challenge. The fatty acid profile of MU1593 is altered compared with wild-type UA159 in all growth conditions tested
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
a specific method for the quantitative determination of beta-glucose 1-phosphate