Information on EC 5.4.2.2 - phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent)

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

EC NUMBER
COMMENTARY hide
5.4.2.2
-
RECOMMENDED NAME
GeneOntology No.
phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
alpha-D-glucose 1-phosphate = D-glucose 6-phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
group transfer
-
-
intramolecular, phosphate group
-
isomerization
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Amino sugar and nucleotide sugar metabolism
-
-
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
D-galactose degradation I (Leloir pathway)
-
-
D-galactose degradation V (Leloir pathway)
-
-
Galactose metabolism
-
-
GDP-glucose biosynthesis
-
-
glucose and glucose-1-phosphate degradation
-
-
glycogen biosynthesis I (from ADP-D-Glucose)
-
-
glycogen degradation I
-
-
glycogen degradation II
-
-
Glycolysis / Gluconeogenesis
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
Pentose phosphate pathway
-
-
Purine metabolism
-
-
Starch and sucrose metabolism
-
-
starch biosynthesis
-
-
starch degradation III
-
-
starch degradation V
-
-
streptomycin biosynthesis
-
-
Streptomycin biosynthesis
-
-
sucrose biosynthesis II
-
-
sucrose degradation II (sucrose synthase)
-
-
sucrose degradation IV (sucrose phosphorylase)
-
-
trehalose degradation V
-
-
UDP-alpha-D-glucose biosynthesis I
-
-
degradation of hexoses
-
-
glycogen metabolism
-
-
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 hide
9001-81-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain Y68
-
-
Manually annotated by BRENDA team
strain Y68
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
bovine
-
-
Manually annotated by BRENDA team
Cassia corymbosa
-
-
-
Manually annotated by BRENDA team
isoform PGM-2, enzyme mRNA expression is mostly up-regulated in the first steps of the response to pollutant exposure and is xenobiotic-dependent
Uniprot
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
gene pgmA
UniProt
Manually annotated by BRENDA team
no activity in Trypanosoma brucei
the organism lost the PGM gene, activity is catalyzed by phosphomannomutase, EC 5.4.2.8 and phospho-N-acetylglucosamine mutase, EC 5.4.2.3
-
-
Manually annotated by BRENDA team
OT3
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain EBY21-8
-
-
Manually annotated by BRENDA team
potato
-
-
Manually annotated by BRENDA team
fragment; strain DJ77
UniProt
Manually annotated by BRENDA team
fragment; strain DJ77
UniProt
Manually annotated by BRENDA team
gene pgmG
UniProt
Manually annotated by BRENDA team
gene pgmG
UniProt
Manually annotated by BRENDA team
spinach
-
-
Manually annotated by BRENDA team
strain K288
-
-
Manually annotated by BRENDA team
strain K288
-
-
Manually annotated by BRENDA team
strain KOD1
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
mung bean
-
-
Manually annotated by BRENDA team
strain KIM5
-
-
Manually annotated by BRENDA team
strain KIM5
-
-
Manually annotated by BRENDA team
additional information
overview prokaryotes and eukaryotes
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
the enzyme belongs to the alpha-D-phosphohexomutase enzyme superfamily
malfunction
metabolism
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
2-deoxyribose 1-phosphate
2-deoxyribose 5-phosphate
show the reaction diagram
-
-
-
-
?
3-phospho-D-glyceric acid
?
show the reaction diagram
-
no mutase activity
-
-
?
alpha-D-glucose 1-phosphate
?
show the reaction diagram
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
show the reaction diagram
alpha-D-glucose 1-phosphate
D-glucose 6-phosphate
show the reaction diagram
alpha-D-glucose 6-phosphate
alpha-D-glucose 1-phosphate
show the reaction diagram
23% of the activity with alpha-D-glucose 1-phosphate
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
show the reaction diagram
alpha-D-mannose 1-phosphate
D-mannose-6-phosphate
show the reaction diagram
alpha-D-mannose-1-phosphate
D-mannose-6-phosphate
show the reaction diagram
-
-
-
-
r
D-fructose-1-phosphate
D-fructose-6-phosphate
show the reaction diagram
-
no mutase activity
-
-
?
D-glucosamine-1-phosphate
D-glucosamine-6-phosphate
show the reaction diagram
-
low enzyme activity
-
-
?
D-glucose 1,6-diphosphate
?
show the reaction diagram
D-glucose 1-phosphate + D-fructose 1,6-diphosphate
D-glucose 1,6-diphosphate + D-fructose 1-phosphate + D-fructose 6-phosphate
show the reaction diagram
-
synthesis of glucose 1,6-diphosphate is an additional activity
synthesis of glucose 1,6-diphosphate is an additional activity
-
D-glucose 6-phosphate
alpha-D-glucose 1-phosphate
show the reaction diagram
D-glucose-1-phosphate
D-glucose-6-phosphate
show the reaction diagram
D-glucose-1-phosphate
glucose-6-phosphate
show the reaction diagram
D-mannose-1-phosphate
D-mannose-6-phosphate
show the reaction diagram
Glucose 1-phosphate + 1,3-bisphosphoglycerate
Glucose 1,6-diphosphate + glycerate 3-phosphate
show the reaction diagram
-
synthesis of glucose 1,6-diphosphate is an additional activity
synthesis of glucose 1,6-diphosphate is an additional activity
-
Glucose 6-phosphate
?
show the reaction diagram
Glucose 6-phosphate
Glucose 1-phosphate
show the reaction diagram
Mannose 1-phosphate
?
show the reaction diagram
-
-
-
-
-
N-acetyl-D-glucosamine-1-phosphate
N-acetyl-D-glucosamine-6-phosphate
show the reaction diagram
-
no mutase activity
-
-
?
additional information
?
-
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
alpha-D-glucose 1-phosphate
?
show the reaction diagram
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
show the reaction diagram
alpha-D-glucose 1-phosphate
D-glucose 6-phosphate
show the reaction diagram
D-glucose 6-phosphate
alpha-D-glucose 1-phosphate
show the reaction diagram
Glucose 6-phosphate
?
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,3-bisphosphoglycerate
-
-
2,3-bisphosphoglycerate
2,6-Difluoroglucose
-
-
3,6-Difluoroglucose
-
-
3-phosphoglycerate
-
uncompetitive inhibition
4,6-Difluoroglucose
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
-
6-Deoxy-6-fluoro-alpha-D-glucopyranosyl phosphate
-
-
alpha-D-galactose 1-phosphate
-
-
alpha-Glucose 1-phosphate-6-vanadate
-
-
alpha-Glucosylfluoride 6-phosphate
-
-
AMP
-
-
cis-aconitate
-
weak inhibition
citrate
-
-
D-fructose 1,6-bisphosphate
-
-
D-fructose 2,6-diphosphate
noncompetitive inhibitor
D-Glucose 1,6-bisphosphate
D-glucose 1-phosphate
D-mannose 1-phosphate
-
-
Disperse Blue 56
-
kinetic studies indicate that it is a parabolic, noncompetitive inhibitor. Reduction of the inhibition in the presence of 0.01% Triton X-100
Enolpyruvate phosphate
-
-
fructose 1,6-diphosphate
fructose 2,6-diphosphate
-
-
isocitrate
-
weak inhibition
N-bromosuccinimide
-
-
p-chloromercuribenzoate
additional information
-
not inhibitory: 1,5-diamino-4,8-dihydroxyanthraquinone
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6-phosphogluconate
-
-
ADP
-
-
alpha-D-Glucose 1,6-bisphosphate
the maximum activity is obtained in the presence of more than 0.2 mM alpha-D-glucose 1,6-bisphosphate; the maximum activity is obtained in the presence of more than 0.2 mM alpha-D-glucose 1,6-bisphosphate
alpha-D-glucose 1,6-diphosphate
cysteine
D-fructose-6-phosphate
-
-
D-glucose-1,6-bisphosphate
EGTA
-
activation
glucose 1,6-bisphosphate
-
absolutely required
GSH
-
required
histidine
Imidazol
-
addition at concentrations below that of Mg2+ increases the activity
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.5
2-deoxyribose-1-phosphate
-
90C
0.0013 - 3.53
alpha-D-glucose 1-phosphate
0.4392 - 0.44
alpha-D-mannose 1-phosphate
0.016 - 0.033
D-Glucose 1,6-bisphosphate
0.00103
D-glucose 1,6-diphosphate
-
in 41 mM 1,3-diaza-2,4-cyclopentadiene /HCl (pH 7.6), 5 mM MgCl2, at 25C
0.018 - 0.02
D-glucose 1-phosphate
2 - 13
D-glucose 6-phosphate
0.0952 - 3
D-glucose-1-phosphate
0.02
D-mannose 1-phosphate
-
25C, pH 7.6
0.0915 - 3.2
D-mannose-1-phosphate
0.022 - 2.6
glucose 1-phosphate
0.017
mannose 1-phosphate
-
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03 - 398
alpha-D-glucose 1-phosphate
59 - 79.17
alpha-D-mannose 1-phosphate
0.74
D-glucose 1,6-diphosphate
Fusarium oxysporum
-
in 41 mM 1,3-diaza-2,4-cyclopentadiene /HCl (pH 7.6), 5 mM MgCl2, at 25C
50 - 135
glucose 1-phosphate
22.5
mannose 1-phosphate
Pseudomonas aeruginosa
-
-
additional information
additional information
Oryctolagus cuniculus
-
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1 - 1188
alpha-D-glucose 1-phosphate
107
714.3
D-glucose 1,6-diphosphate
Fusarium oxysporum
-
in 41 mM 1,3-diaza-2,4-cyclopentadiene /HCl (pH 7.6), 5 mM MgCl2, at 25C
2898
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
48
D-fructose 1,6-bisphoshate
-
pH 7.2, 30C
-
0.23
D-Glucose 1,6-bisphosphate
-
25C, pH 7.6, substrate inhibition at high concentrations
3.3
D-glucose 1-phosphate
-
25C, pH 7.6, substrate inhibition at high concentrations
1.35
D-mannose 1-phosphate
-
25C, pH 7.6, substrate inhibition at high concentrations
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.01
-
pH 7.0, 37C, activity in undialyzed cell extracts
0.1 - 1
-
purified recombinant His-tagged Pgm3, pH 7.5, 30C
0.24
-
purified recombinant His-tagged Pgm1, pH 7.5, 30C
0.8
-
cell extract, pH 7.0
1.1
-
crude enzyme, at pH 7.6, 25C
5
aerobic condition; aerobic conditiones
5.3
-
after 5fold purification, at pH 7.6, 25C
6.53
O2 deprivation for 24 h
11.4
-
substrate mannose 1-phosphate
11.7
-
-
28
-
substrate glucose 1-phosphate
31.5
-
substrate glucose 1-phosphate
33.7
-
purified recombinant His-tagged Pgm2, pH 7.5, 30C
40.2
-
isozyme PGM2, substrate glucose 1-phosphate
42
-
isozyme PGM2, substrate glucose 1-phosphate
67.5
purified recombinant enzyme, pH 7.4, 30C
76
-
PGM2, using alpha-D-glucose 1-phosphate as substrate, in 50 mM HEPES, pH 7.1, 5 mM MgCl2, at 30C
84
isozyme PGM-II, using alpha-D-glucose 1-phosphate as substrate, in 50 mM HEPES-KOH, pH 8.0, at 37C
87
-
PGM1, using alpha-D-glucose 1-phosphate as substrate, in 50 mM HEPES, pH 7.1, 5 mM MgCl2, at 30C
128
-
recombinant PGM
156.9
-
substrate glucose 1-phosphate
205
-
substrate glucose 1-phosphate
286
-
substrate glucose 1-phosphate
338
isozyme PGM-I, using alpha-D-glucose 1-phosphate as substrate, in 50 mM HEPES-KOH, pH 8.0, at 37C
420
-
purified enzyme, pH 7.0, 90C
490
-
substrate glucose 1-phosphate
1263
-
isozyme PGM1, substrate glucose 1-phosphate
1442
-
isozyme PGM1, substrate glucose 1-phosphate
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.6 - 7.5
-
more than 50% of maximum activity within this range
7.4 - 7.6
-
-
7.4 - 8
-
depending on the substrate
7.5
Cassia corymbosa
-
-
7.5 - 9.2
-
crude enzyme form
7.8 - 7.9
-
-
8.1
-
phosphoglucomutase I and II
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
-
using 3-(N-morpholino)propanesulfonic acid buffer, the enzyme retains up to 90% of its initial activity
6.8 - 8.3
Cassia corymbosa
-
less than 50% of maximal activity above and below
7.5 - 8.6
-
phosphoglucomutase II
7.5 - 9
-
phosphoglucomutase I
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 40
recombinant enzyme
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5
-
isoelectric focusing
5.47
deduced from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
inhibition of phosphoglucomutase activity by chronic treatment with Li+ causes alterations of glucose-phosphate level with compensatory elevation of phosphoglucomutase activity
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
low enzyme expression in hemolymph
Manually annotated by BRENDA team
-
inhibition of phosphoglucomutase activity by chronic treatment with Li+ causes compensatory elevation of phosphoglucomutase activity in Li+-treated bipolar patients due to increased expression of PGM1 gene
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Lactococcus lactis subsp. cremoris (strain MG1363)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
Xanthomonas axonopodis pv. citri (strain 306)
Xanthomonas axonopodis pv. citri (strain 306)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28000
-
3 * 28276, calculated, 3 * 28000, SDS-PAGE
28276
-
3 * 28276, calculated, 3 * 28000, SDS-PAGE
29880
-
calculated
30000
-
SDS-PAGE of purified alpha-PGM, with His-tag
31633
-
2 * 31633, sedimentation equilibrium in 6 M guanidine-HCl, sedimentation equilibrium in dodecyl sulfate and 2-mercaptoethanol, SDS-PAGE
47000
-
FPLC gel filtration
49800
x * 49800, about, sequence calculation
49850
-
4 * 49850, protein encoded by gene TK1108, calculated
50000
-
SDS-PAGE
52000
-
1 * 52000, SDS-PAGE
56000
-
1 * 56000, SDS-PAGE
57500
deduced from amino acid sequence
58000 - 60000
Cassia corymbosa
-
gel filtration, sucrose density gradient centrifugation
58500
-
isozyme PGM1, gel filtration, SDS-PAGE
59000
-
1 * 59000 + 1 * 67000
59500
native enzyme, non-denaturing PAGE
60800
2 * 60800, calculated from amino acid sequence
61000
x * 61000, calculated
63000
x * 63000, deduced from nucleotide sequence
64900
-
estimated from amino acid sequence
65600
-
gel filtration, sucrose density gradient centrifugation, sedimentation equilibrium centrifugation
67000
-
1 * 59000 + 1 * 67000
69000
-
isozyme PGM2, gel filtration, SDS-PAGE
73000
-
1 * 73000, SDS-PAGE
84300
-
gel filtration
125000
-
gel filtration
130000
-
phosphoglucomutase I and II, gel filtration
132000
133000
-
gel filtration
210000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
monomer
tetramer
-
4 * 49850, protein encoded by gene TK1108, calculated
trimer
-
3 * 28276, calculated, 3 * 28000, SDS-PAGE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
additional information
-
phosphoprotein, 1 mol phosphate per mol of enzyme
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystallized with vapor diffusion, streak seeding, in ammonium sulfate solution, optimized crystals diffract to 1.5 A resolution
-
crystal structure at 2.7 A resolution
-
crystallization procedure, polyethyleneglycol-400, 1-4.5% must be included in crystal growth medium
-
production of active enzyme-substrate/product complexes
-
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
-
in complex with inhibitor xylose 1-phosphate or slow substrate ribose 1-phosphate. Both ligands induce an interdomain rearrangement, using different enzyme-ligand interactions
-
phospho- and dephospho-enzyme in complex with reaction intermediate glucose 1,6-bisphosphate at 1.9 and 2.0 A
-
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
-
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
-
hanging drop vapor diffusion method, using 0.1 M Bis-Tris, pH 6.5, 0.2 M MgCl2, and 25% (w/v) PEG 3350
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 7.4
-
-
3295
6.5 - 7.4
purified recombinant enzyme, stable at
728738
7 - 10
-
at pH 7.0 only 17.5% of the relative activity is recovered, the enzyme retains 14% of its initial activity after incubation at pH 10.0
714859
8
-
unstable above
3281
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
-
12 h, 30% loss of activity
30 - 60
-
PGM is almost stable (12% loss of the activity) at 30C for 60 min, while almost complete loss of activity is observed at 50 and 60C after 10 min
41
-
at least 5 min stable
60 - 70
-
at 60C PGM is relatively stable and loses 10% of its initial activity after incubation for 8 h. At 70C, it deactivates quickly with a half-life of 0.8 h. PGM at a concentration of 500 nM has a half-life of 30 h at 60C, while 2 nM or 50 nM PGM loses nearly 100% of activity within 12 h. Thermostability of PGM at a low concentration (2 nM, 100 units/l) is enhanced by 12fold at 60C with addition of 1 mg/ml bovine serum albumin, 0.1% (v/v) Triton X-100, 5 mM Mg2+, and 0.5 mM Mn2+
65
-
30 min, 90% loss of activity
95
-
longer than 90 min stable
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
at pH 7.5, the PGM activity in the HEPES buffer is 20% lower than in the Tris-HCl buffer
-
extremely unstable in crude extracts, protease sensitive, Bacillus subtilis 168 SR 22 can be used as a protease-negative mutant
-
freezing and thawing results in almost total loss of activity, freeze-dried enzyme stable
-
loss of activity is observed when phosphate buffer is used in the pH range of 6.0-8.0
-
stable in 5 mM acetate buffer or 10 mM citrate buffer, pH 5.5, 4 C, but in 5 mM Tris-HCl buffer pH 7.4, 80% loss of activity per day
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70C, requires EDTA to restore activity after storage
-
-80C, fast-frozen in LN2 and stored for 2 years without affecting the sample homogeneity
-
0-4C, 50% glycerol, 2-3 d, no loss of activity
-
4-6C, 0.05 M acetate buffer, pH 5.0, crystalline enzyme form, many months stable
-
4C, crude enzyme extract, 0.2 mM EDTA, 10% glycerol, pH 6.5, 3-4 weeks stable
-
4C, purified enzyme, 75% saturated ammonium sulfate, 0.2 mM EDTA, 10% glycerol, pH 6.5, 3 months stable
-
4C, saturated ammonium sulfate, 0.1 M Na2HPO4-HCl, pH 7.0, 0.1 mM EDTA, 1 mM Mg2+, 3 months stable
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 isozymes
-
ammonium sulfate, Sephadex G-25, DEAE-Toyopearl, Toyopearl HW-65
-
both native and recombiant enzyme
-
glutathione Sepharose column chromatography; glutathione Sepharose column chromatography
heat treatment 85C, 20 min, anion-exchange, hydrophobic and gel filtration column chromatography
-
His-Select Ni-Affinity gel column chromatography, gel filtration
isozymes PGM1 and PGM2
-
Ni-chelating resin chromatography
Ni-Sepharose affinity column chromatography
-
Ni2+-NTA column chromatography
-
nickel-affinity column chromatography
-
partial
Q-Sepharose column chromatography and Sephacryl-S 100 gel filtration
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3), removal of the His-tag, purification by nickel affinity chromatography and dialysis
-
recombinant His-tagged Pgm1, Pgm2, and Pgm3 from Escherichia coli strain BL21 (DE3)
-
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, protein refolding, and ultrafiltration
recombinant PGM
recombinant protein is purified by centrifugation und affinity chromatography with Ni-NTA Superflow cartridge. Purity is assessed by SDS-PAGE
-
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
-
ultracentrifugation
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloned and homologously overexpressed in Lactococcus lactis subsp. cremoris strain NZ9000, introducing 6xHis-tag
-
expressed in Eascherichia coli and Saccharomyces cerevisiae BY4741 wild type and pgm1DELTA/pgm2DELTA mutant strain
-
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells; expressed in Escherichia coli BL21(DE3) cells
expressed in Saccharomyces cerevisiae strain JF645
-
expression in Agrobacterium tumefaciens; expression in Agrobacterium tumefaciens; expression in Agrobacterium tumefaciens
expression in Escherichia coli
expression of cytosolic and plastidial isozymes in Nicotiana tabacum cv. Xanthi using the cauliflower mosaic virus 35S promoter. The transgenic plants expressing Arabidopsis plastidial PGM show 3.5-8.2fold higher enzyme activity compared to the wild-type, and leaf starch and sucrose contents increase 2.3-3.2fold and 1.3-1.4fold, respectively over wild-type levels, while transgenic plants expressing Arabidopsis cytosolic PGM show a 2.1-3.4fold increase in PGM activity over wild-type and a decrease of leaf starch content, but no change in sucrose content
-
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)
-
gene pgmA, sequence comparison, phylogenetic analysis and expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3) in inclusion bodies
gene pgmG, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, overexpression of the His-tagged enzyme in Escherichia coli strain BL21(DE3), cloning in Escherichia coli strain DH5alpha
genes pgm1, pgm2, and pgm3, cloning in Escherichia coli strain DH5alpha, expression of His-tagged enzymes in Escherichia coli strain BL21 (DE3)
-
overexpression in Escherichia coli
overexpression of histidine-tagged fusion protein in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
high SpgM expression is correlated with the lactams ceftazidime, ticarcillin/clavulanic acid, and piperacillin/tazobactam
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H109Q
6% of wild-type activity
H308N
100% of wild-type activity
H308N/H329N
5% of wild-type activity
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
H329N
6% of wild-type activity
K118L
4% of wild-type activity
K118L/H109Q
5% of wild-type activity
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
R241C
-
0.3% of wild-type acivity, with Km value similar to wild-type
S108A
12% of wild-type activity
S108A/H109Q
6% of wild-type activity
S108A/H308N
3% of wild-type activity
S108A/H329N
no activity
S108D
7% of wild-type activity
S108V
1% of wild-type activity
S309A
activity of mutant enzyme with D-glucose 6-phosphate is 58% compared to activity of wild-type enzyme
S309D
activity of mutant enzyme with D-glucose 6-phosphate is 4% compared to activity of wild-type enzyme
S309N
activity of mutant enzyme with D-glucose 6-phosphate is 27% compared to activity of wild-type enzyme
S309Q
activity of mutant enzyme with D-glucose 6-phosphate is 22% compared to activity of wild-type enzyme
S309T
activity of mutant enzyme with D-glucose 6-phosphate is 36% compared to activity of wild-type enzyme
S309V
activity of mutant enzyme with D-glucose 6-phosphate is 36% compared to activity of wild-type enzyme
S309A
-
activity of mutant enzyme with D-glucose 6-phosphate is 58% compared to activity of wild-type enzyme
-
S309N
-
activity of mutant enzyme with D-glucose 6-phosphate is 27% compared to activity of wild-type enzyme
-
S309Q
-
activity of mutant enzyme with D-glucose 6-phosphate is 22% compared to activity of wild-type enzyme
-
S309T
-
activity of mutant enzyme with D-glucose 6-phosphate is 36% compared to activity of wild-type enzyme
-
S309V
-
activity of mutant enzyme with D-glucose 6-phosphate is 36% compared to activity of wild-type enzyme
-
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) inclusion bodies
reversible denaturation in 5 M urea
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
food industry
medicine
-
inhibition of phosphoglucomutase activity by chronic treatment with Li+ causes compensatory elevation of phosphoglucomutase activity in Li+-treated bipolar patients due to increased expression of PGM1 gene
molecular biology
-
phosphoglucomutase is a very suitable marker for analysis of the inter-breed and intra-breed polymorphism for the mulberry silkworm, and for determining the level of genetic variability
Show AA Sequence (4912 entries)
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