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 ACCESSION NO.
LITERATURE
N-acetyl-alpha-D-glucosamine 1-phosphate = N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
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 ACCESSION NO.
COMMENTARY
LITERATURE
group transfer
-
-
intramolecular, phosphate group
-
isomerization
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Amino sugar and nucleotide sugar metabolism
-
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 ACCESSION NO.
COMMENTARY
LITERATURE
2-Acetamido-2-deoxy-D-glucose-1,6-bisphosphate:2-acetamido-2-deoxy-D-glucose 1-phosphate phosphotransferase
-
-
-
-
Acetylaminodeoxyglucose phosphomutase
-
-
-
-
Acetylglucosamine phosphomutase
-
-
-
-
CaAGM1
Q9P4V2
-
DNA-damage-repair/toleration protein DRT101
-
-
-
-
EC 2.7.5.2.
-
-
formerly
-
HsAGM1
O95394
-
N-acetylglucosamine-phosphate mutase
-
-
-
-
PAGM
-
-
-
-
PAGM
Q58I85
-
PGlcNAc mutase
-
-
-
-
Phospho-N-acetylglucosamine mutase
-
-
-
-
Phosphomutase, acetylglucosamine
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9027-51-4
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
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-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-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
-
-
-
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
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-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
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
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
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 ACCESSION NO.
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
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 ACCESSION NO.
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]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
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
-
0.0237
-
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]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.79
-
N-acetyl-alpha-D-glucosamine
O95394
-
2.94
-
N-acetyl-alpha-D-glucosamine
O95394
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.056
-
-
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
7
-
Tris-HCl buffer
7
7.5
-
Tris-maleate buffer
7.3
-
-
Tris-acetate buffer
7.9
-
-
formation of N-acetylglucosamine 1-phosphate
8.2
-
-
Tris-HCl buffer
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
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
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
59000
-
-
gel filtration
60000
-
-
gel filtration
60600
-
-, Q58I85
SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
monomer
-
1 * 64000, SDS-PAGE
monomer
-
1 * 60000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
enzyme is present in two forms of different heat stability
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
purified enzyme loses more than 90% activity upon one freezing and thawing
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
LITERATURE
glutathione affinity column
-, Q58I85
recombinant CaAgm1-GST fusion protein
-
recombinant HsAgm1-GST fusion protein
O95394
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
-, Q58I85
expression as glutathione S-transferase fusion protein
-
expression in Escherichia coli
-
expression in Escherichia coli
O95394
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
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
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
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