Information on EC 5.4.2.3 - phosphoacetylglucosamine mutase

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY
5.4.2.3
-
RECOMMENDED NAME
GeneOntology No.
phosphoacetylglucosamine mutase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N-acetyl-alpha-D-glucosamine 1-phosphate = N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
ping-pong mechanism
-
N-acetyl-alpha-D-glucosamine 1-phosphate = N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
the N-acetyl group of the substrate is recognized by V370 and N389 in domain 3, from which the substrate specificity arises. Substrate rotates about 180 on the axis linking C4 and the midpoint of the C5-O5 bond in the reaction
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
isomerization
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Amino sugar and nucleotide sugar metabolism
-
-
Biosynthesis of antibiotics
-
-
chitin derivatives degradation
-
-
UDP-N-acetyl-D-galactosamine biosynthesis II
-
-
UDP-N-acetyl-D-glucosamine biosynthesis II
-
-
SYSTEMATIC NAME
IUBMB Comments
N-Acetyl-alpha-D-glucosamine 1,6-phosphomutase
The enzyme is activated by N-acetyl-alpha-D-glucosamine 1,6-bisphosphate.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2-Acetamido-2-deoxy-D-glucose-1,6-bisphosphate:2-acetamido-2-deoxy-D-glucose 1-phosphate phosphotransferase
-
-
-
-
Acetylaminodeoxyglucose phosphomutase
-
-
-
-
Acetylglucosamine phosphomutase
-
-
-
-
DNA-damage-repair/toleration protein DRT101
-
-
-
-
N-acetylglucosamine-phosphate mutase
-
-
-
-
PAGM
-
-
-
-
PGlcNAc mutase
-
-
-
-
Phospho-N-acetylglucosamine mutase
-
-
-
-
Phosphomutase, acetylglucosamine
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9027-51-4
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Coffea sp.
coffee plant
-
-
Manually annotated by BRENDA team
strain MR4
-
-
Manually annotated by BRENDA team
Giardia intestinalis MR4
strain MR4
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
gene PAGM
UniProt
Manually annotated by BRENDA team
Trypanosoma brucei 427
gene PAGM
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
F4NCC3
the enzyme belongs to the alpha-D-phosphohexomutase superfamily of enzymes
evolution
Trypanosoma brucei 427
-
the enzyme belongs to the alpha-D-phosphohexomutase superfamily of enzymes
-
malfunction
Q9VTZ4
loss-of-function mutations in the nst gene, which encodes PGM3, block fibroblast growth factor signaling during embryonic mesoderm and tracheal development. In nst mutants with an 80% reduction in the amount of UDP-GlcNAc, O-GlcNAcylation is compromised. Embryos maternally and zygotically mutant for nst exhibit defects in mesoderm layer formation during gastrulation that are similar to those observed in embryos with mutations in the gene encoding the fibroblast growth factor receptor Heartless (Htl). Zygotic nst mutants (nstZ) exhibit normal dorsal mesoderm differentiation, embryos homozygous for the hypomorphic htlYY262 allele show a reduction in dorsal mesoderm. Phenotypes, overview. Dof is the critical component in MAPK activation affected in nst mutants
metabolism
Q9VTZ4
Nst acts downstream of fibroblast growth factor receptor signaling
physiological function
F4NCC3
the enzyme is essential for parasite growth. It takes over the function of phosphoglucomutase, EC 5.4.2.2, whose gene is lost in Trypanosoma brucei, together with phosphomannomutase, EC 5.4.2.8, producing D-glucose 1-phosphate from D-glucose 6-phosphate, kinetics, overview
physiological function
Q9VTZ4
the enzyme is required for normal cellular levels of UDP-GlcNAc and essential in UDP-GlcNAc biosynthesis, and for fibroblast growth factor signaling in early embryos. Role for Nst in fibroblast growth factor receptor Heartless (Htl) signaling
physiological function
Trypanosoma brucei 427
-
the enzyme is essential for parasite growth. It takes over the function of phosphoglucomutase, EC 5.4.2.2, whose gene is lost in Trypanosoma brucei, together with phosphomannomutase, EC 5.4.2.8, producing D-glucose 1-phosphate from D-glucose 6-phosphate, kinetics, overview
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-glucose-1-phosphate
D-glucose-6-phosphate
show the reaction diagram
Q58I85
-
-
-
?
Glucose 1-phosphate
Glucose 6-phosphate
show the reaction diagram
-
-
-
-
Glucose 1-phosphate
Glucose 6-phosphate
show the reaction diagram
-
-
-
-
N-acetyl-alpha-D-glucosamine 1-phosphate
N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
O95394
-
-
?
N-acetyl-alpha-D-glucosamine 1-phosphate
N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
Q9P4V2
-
-
?
N-acetyl-alpha-D-glucosamine 1-phosphate
N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
Trypanosoma brucei, Trypanosoma brucei 427
F4NCC3
-
-
-
r
N-Acetyl-D-glucosamine 1-phosphate
N-Acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
-
N-Acetyl-D-glucosamine 1-phosphate
N-Acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
-
N-Acetyl-D-glucosamine 1-phosphate
N-Acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
specific for the alpha-1-phosphate anomer
-
-
-
N-Acetyl-D-glucosamine 1-phosphate
N-Acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
in presence of N-acetylglucosamine 1,6-diphosphate
-
-
N-acetyl-D-glucosamine 6-phosphate
N-acetyl-alpha-D-glucosamine 1-phosphate
show the reaction diagram
F4NCC3
-
-
-
r
N-acetyl-D-glucosamine 6-phosphate
N-acetyl-alpha-D-glucosamine 1-phosphate
show the reaction diagram
Q9VTZ4
-
-
-
r
N-acetyl-D-glucosamine 6-phosphate
N-acetyl-alpha-D-glucosamine 1-phosphate
show the reaction diagram
Trypanosoma brucei 427
F4NCC3
-
-
-
r
N-Acetylglucosamine 6-phosphate
N-Acetylglucosamine 1-phosphate
show the reaction diagram
-
-
-
-
N-Acetylglucosamine 6-phosphate
N-Acetylglucosamine 1-phosphate
show the reaction diagram
-
-
-
-
N-Acetylglucosamine 6-phosphate
N-Acetylglucosamine 1-phosphate
show the reaction diagram
Coffea sp.
-
-
-
-
N-Acetylglucosamine 6-phosphate
?
show the reaction diagram
-
the reaction is involved in the synthesis of active glycosyl intermediates in reticulo-endothelial tissues
-
-
-
N-Acetylglucosamine 6-phosphate
?
show the reaction diagram
-
enzyme is involved in galactosamine synthesis from glucose during encystment, induced during encystment
-
-
-
N-Acetylglucosamine 6-phosphate
?
show the reaction diagram
Coffea sp.
-
enzyme in the pathway of UDP-N-acetyl-D-glucosamine formation
-
-
-
N-Acetylglucosamine 6-phosphate
?
show the reaction diagram
Giardia intestinalis MR4
-
enzyme is involved in galactosamine synthesis from glucose during encystment, induced during encystment
-
-
-
N-acetylglucosamine-1-phosphate
N-acetylglucosamine-6-phosphate
show the reaction diagram
Q58I85
-
-
-
?
Glucose 1-phosphate
Glucose 6-phosphate
show the reaction diagram
-
in presence of glucose 1,6-diphosphate
-
-
additional information
?
-
-
one of the two last pathway-specific enzymes of hexosamine biosynthesis. The hexosamine pathway is regulated at the post-translational level during zoospore germination
-
-
-
additional information
?
-
Trypanosoma brucei, Trypanosoma brucei 427
F4NCC3
the enzyme exhibits the function of phosphoglucomutase, EC 5.4.2.2, whose gene is lost in Trypanosoma brucei, together with phosphomannomutase, EC 5.4.2.8, producing D-glucose 1-phosphate from D-glucose 6-phosphate, kinetics, overview
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
N-acetyl-alpha-D-glucosamine 1-phosphate
N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
O95394
-
-
?
N-acetyl-alpha-D-glucosamine 1-phosphate
N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
Q9P4V2
-
-
?
N-acetyl-alpha-D-glucosamine 1-phosphate
N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
Trypanosoma brucei, Trypanosoma brucei 427
F4NCC3
-
-
-
r
N-acetyl-D-glucosamine 6-phosphate
N-acetyl-alpha-D-glucosamine 1-phosphate
show the reaction diagram
Q9VTZ4
-
-
-
r
N-Acetylglucosamine 6-phosphate
?
show the reaction diagram
-
the reaction is involved in the synthesis of active glycosyl intermediates in reticulo-endothelial tissues
-
-
-
N-Acetylglucosamine 6-phosphate
?
show the reaction diagram
-
enzyme is involved in galactosamine synthesis from glucose during encystment, induced during encystment
-
-
-
N-Acetylglucosamine 6-phosphate
?
show the reaction diagram
Coffea sp.
-
enzyme in the pathway of UDP-N-acetyl-D-glucosamine formation
-
-
-
N-Acetylglucosamine 6-phosphate
?
show the reaction diagram
Giardia intestinalis MR4
-
enzyme is involved in galactosamine synthesis from glucose during encystment, induced during encystment
-
-
-
additional information
?
-
-
one of the two last pathway-specific enzymes of hexosamine biosynthesis. The hexosamine pathway is regulated at the post-translational level during zoospore germination
-
-
-
additional information
?
-
Trypanosoma brucei, Trypanosoma brucei 427
F4NCC3
the enzyme exhibits the function of phosphoglucomutase, EC 5.4.2.2, whose gene is lost in Trypanosoma brucei, together with phosphomannomutase, EC 5.4.2.8, producing D-glucose 1-phosphate from D-glucose 6-phosphate, kinetics, overview
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
-
required, Km: 1.2 mM
Mg2+
-
divalent metal ion required. Optimal Mg2+ concentration in the presence of dithiothreitol is 10 mM, maximal activity with other metal chelators is obtained with 1 mM Mg2+
Mg2+
-
1 mM, required
Mg2+
F4NCC3
required
Mn2+
-
divalent metal ion required. Mn2+ is less efficient than Mg2+
phosphate
-
covalently linked to the enzyme. The phosphate-protein linkage is stable in mild acid, at 50 C for up to 2 h. However phosphate is completely released under mild alkaline conditions at 50 C within 1 h
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Be2+
-
0.02 mM in presence of 1 mM Mg2+, complete inhibition
Cd2+
-
0.5 mM in presence of 1 mM Mg2+, complete inhibition
Cu2+
-
0.5 mM in presence of 1 mM Mg2+, complete inhibition
D-glucose 1-phosphate
F4NCC3
competitive inhibition
D-glucose 6-phosphate
F4NCC3
competitive inhibition
Mn2+
-
1 mM in presence of 1 mM Mg2+, complete inhibition
Zn2+
-
0.5 mM in presence of 1 mM Mg2+, complete inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
8-hydroxyquinoline
-
metal chelator required
Cys
-
metal chelator required
diethyldithiocarbamate
-
metal chelator required
diethyldithiocarbamide
-
or histidine required for maximal activity
-
fructose 1,6-diphosphate
-
or glucose 1,6-diphosphate activates, Km: 0.018 mM
glucose 1,6-diphosphate
-
required, Km: 0.03 mM
glucose 1,6-diphosphate
-
required for reaction with glucose 1-phosphate, Km: 0.025 mM
glucose 1,6-diphosphate
-
required, maximal activity at 0.005-0.05 mM
glucose 1,6-diphosphate
-
or fructose 1,6-diphosphate activates, Km: 0.002 mM
glucose 1,6-diphosphate
-
required, maximal activity at 0.05 mM
N-Acetylglucosamine 1,6-diphosphate
-
required for reaction with N-acetylglucosamine 1-phosphate
sulfhydryl compound
-
increases activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.54
D-glucose-1-phosphate
Q58I85
pH 7.4, 26C
0.39
glucose 1-phosphate
-
-
0.658
glucose 1-phosphate
-
-
0.046
N-acetyl-alpha-D-glucosamine
O95394
-
0.014
N-acetyl-D-glucosamine 6-phosphate
F4NCC3
pH 7.3, 37C
0.0237
N-acetylglucosamine 1-phosphate
-
-
0.29
N-acetylglucosamine 1-phosphate
-
-
0.7
N-acetylglucosamine 1-phosphate
-
-
3.6
N-acetylglucosamine 6-phosphate
-
-
0.046
N-acetylglucosamine-1-phosphate
Q58I85
pH 7.4, 26C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.79
N-acetyl-alpha-D-glucosamine
O95394
-
2.94
N-acetyl-alpha-D-glucosamine
O95394
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
16
N-acetyl-D-glucosamine 6-phosphate
F4NCC3
pH 7.3, 37C
1092
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0063
D-glucose 1-phosphate
F4NCC3
versus N-acetyl-D-glucosamine 6-phosphate, pH 7.3, 37C
0.0083
D-glucose 6-phosphate
F4NCC3
versus N-acetyl-D-glucosamine 6-phosphate, pH 7.3, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.056
-
-
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 7
-
Tris-HCl buffer
7 - 7.5
-
Tris-maleate buffer
7.2 - 9.1
F4NCC3
broad optimum
7.3
-
Tris-acetate buffer
7.9
-
formation of N-acetylglucosamine 1-phosphate
8.2
-
Tris-HCl buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 9
-
pH 6.5: about 45% of maximal activity, pH 9.0: about 40% of maximal activity, Tris-maleate buffer
7 - 8.5
-
about 60% of maximal activity at pH 7.0 and at pH 8.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
F4NCC3
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
induced during encystment
Manually annotated by BRENDA team
Giardia intestinalis MR4
-
induced during encystment
-
Manually annotated by BRENDA team
Coffea sp.
-
-
Manually annotated by BRENDA team
-
highest activity of reticulo-endothelial tissues tested
Manually annotated by BRENDA team
Giardia intestinalis MR4
-
-
-
Manually annotated by BRENDA team
additional information
F4NCC3
quantitative proteomic analysis show that the TbPAGM protein is present in both life cycle stages, procyclic and bloodstream forms
Manually annotated by BRENDA team
additional information
Trypanosoma brucei 427
-
quantitative proteomic analysis show that the TbPAGM protein is present in both life cycle stages, procyclic and bloodstream forms
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Trypanosoma brucei 427
-
-
-
Manually annotated by BRENDA team
Trypanosoma brucei 427
-
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
59000
-
gel filtration
3296
60000
-
gel filtration
677345
60600
Q58I85
SDS-PAGE
661887
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
-
1 * 60000, SDS-PAGE
monomer
-
1 * 64000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
both in apo form and in the complex forms with substrate and product. Protein consists of four domains. of which three domains have essentially the same fold. The catalytic cleft is formed by four loops from each domains. The N-acetyl group of the substrate is recognized by V370 and N389 in domain 3, from which the substrate specificity arises. Substrate rotates about 180 on the axis linking C4 and the midpoint of the C5-O5 bond in the reaction
-
space group P21, crystal diffract to beyond 1.8 A
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
enzyme is present in two forms of different heat stability
3296
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
purified enzyme loses more than 90% activity upon one freezing and thawing
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-16C, stable for several months
-
0-4C, pH 6.5, stable for 7 days
-
0C, 30% sucrose or 30% glycerol, 50% loss of activity after 3 weeks. Addition of albumin or varying the pH does not appreciably enhance the stability of the enzyme
-
frozen enzyme, pH 6.5, stable for at least 1 month
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
glutathione affinity column
Q58I85
recombinant CaAgm1-GST fusion protein
-
recombinant HsAgm1-GST fusion protein
O95394
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
F4NCC3
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
Q58I85
expression as glutathione S-transferase fusion protein
-
expression in Escherichia coli
-
gene nst, DNA and amino acid sequence determination, gene nst is allelic to CG10627, expression analysis
Q9VTZ4
expression in Escherichia coli
O95394
gene PAGM, DNA and amino acid sequence determination and analysis, expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
F4NCC3
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D276A
O95394
no activity
D276E
O95394
extremely low activity
D278A
O95394
no activity
D278E
O95394
no activity
D280A
O95394
extremely low activity
D70A
O95394
65% of wild type activity
G277A
O95394
79% of wild type activity
G499A
O95394
0.5% of wild type activity
G58A
O95394
20% of wild type activity
G72A
O95394
3% of wild type activity
H65A
O95394
no activity
H65R
O95394
very low activity
K74A
O95394
no activity
N66A
O95394
1.3% of wild type activity
P67A
O95394
100% of wild type activity
R281A
O95394
no activity
R281K
O95394
no activity
R496A
O95394
extremely low activity
R498A
O95394
8% of wild type activity
S64A
O95394
no activity
S64T
O95394
no activity
T500A
O95394
extremely low activity
T62A
O95394
106% of wild type activity
additional information
F4NCC3
RNAi knockdown of gene TbPAGM, construction of a cell line expressing tetracycline inducible double-stranded RNA targeting TbPMM, induction of dsRNA targeting TbPMM results in a 68% knockdown of TbPMM mRNA after 48 h and a reduction of growth rate that leads to cell death after 72 h, phenotypes, overview
additional information
Trypanosoma brucei 427
-
RNAi knockdown of gene TbPAGM, construction of a cell line expressing tetracycline inducible double-stranded RNA targeting TbPMM, induction of dsRNA targeting TbPMM results in a 68% knockdown of TbPMM mRNA after 48 h and a reduction of growth rate that leads to cell death after 72 h, phenotypes, overview
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
-
enzymic synthesis of beta-UDP-N-acetylglucosamine using UTP:N-acetylglucosamine 1-phosphate phosphotransferase and N-acetyl-D-glucosamine 1,6-phosphomutase