Information on EC 5.4.2.10 - phosphoglucosamine mutase

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

EC NUMBER
COMMENTARY hide
5.4.2.10
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RECOMMENDED NAME
GeneOntology No.
phosphoglucosamine mutase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate
show the reaction diagram
The enzyme is involved in the pathway for bacterial cell-wall peptidoglycan and lipopolysaccharide biosynthesis, being an essential step in the pathway for UDP-N-acetylglucosamine biosynthesis. The enzyme from E. coli is activated by phosphorylation and can be autophosphorylated in vitro by glucosamine 1,6-bisphosphate, which is an intermediate in the reaction, glucose 1,6-bisphosphate or ATP. It can also catalyse the interconversion of glucose 1-phosphate and glucose 6-phosphate, although at a much lower rate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isomerization
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Amino sugar and nucleotide sugar metabolism
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anhydromuropeptides recycling
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Biosynthesis of antibiotics
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CMP-legionaminate biosynthesis I
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Metabolic pathways
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UDP-GlcNAc biosynthesis
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UDP-N-acetyl-D-glucosamine biosynthesis I
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SYSTEMATIC NAME
IUBMB Comments
alpha-D-glucosamine 1,6-phosphomutase
The enzyme is involved in the pathway for bacterial cell-wall peptidoglycan and lipopolysaccharide biosyntheses, being an essential step in the pathway for UDP-N-acetylglucosamine biosynthesis. The enzyme from Escherichia coli is activated by phosphorylation and can be autophosphorylated in vitro by alpha-D-glucosamine 1,6-bisphosphate, which is an intermediate in the reaction, alpha-D-glucose 1,6-bisphosphate or ATP. It can also catalyse the interconversion of alpha-D-glucose 1-phosphate and glucose 6-phosphate, although at a much lower rate.
CAS REGISTRY NUMBER
COMMENTARY hide
9031-92-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
constitutive gene glmM
UniProt
Manually annotated by BRENDA team
strain 900
UniProt
Manually annotated by BRENDA team
strain 900
UniProt
Manually annotated by BRENDA team
gene glmM
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-
Manually annotated by BRENDA team
gene glmM
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-
Manually annotated by BRENDA team
strain UA159
UniProt
Manually annotated by BRENDA team
strain UA159
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-D-glucosamine 1-phosphate
D-glucosamine 6-phosphate
show the reaction diagram
alpha-D-glucosamine 6-phosphate
alpha-D-glucosamine 1-phosphate
show the reaction diagram
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
show the reaction diagram
D-glucoamine 6-phosphate
D-glucosamine 1-phosphate
show the reaction diagram
D-glucosamine 1-phosphate
D-glucosamine 6-phosphate
show the reaction diagram
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-
r
D-glucosamine 6-phosphate
D-glucosamine 1-phosphate
show the reaction diagram
D-glucose 1-phosphate
D-glucose 6-phosphate
show the reaction diagram
D-Mannose 1-phosphate
D-Mannose 6-phosphate
show the reaction diagram
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5fold lower activity than phosphoglucosamine mutase activity
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?
additional information
?
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activity of GlmU and GlmM from Lactobacillus casei in a coupled enzymatic assay
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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-glucosamine 1-phosphate
D-glucosamine 6-phosphate
show the reaction diagram
D-glucoamine 6-phosphate
D-glucosamine 1-phosphate
show the reaction diagram
D-glucosamine 1-phosphate
D-glucosamine 6-phosphate
show the reaction diagram
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-
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r
D-glucosamine 6-phosphate
D-glucosamine 1-phosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
required for activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
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80% reduced activity
EDTA
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abolishes autophosphorylation and catalytic activity
Mn2+
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80% reduced activity
Zn2+
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efficient autophosphorylation, but absence of catalytic activity
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-fructose-1,6-bisphosphate
required to activate the enzyme
D-glucosamine 1,6-diphosphate
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retains the enzyme in an active and phosphorylated form
D-glucose 1,6-diphosphate
dithiothreitol
1 mM, required for maximal activity
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.08
D-glucosamine 1,6-diphosphate
0.05
D-Glucosamine 6-phosphate
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0.5
D-glucose 1,6-diphosphate
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0.08 - 0.65
D-glucose 1-phosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.52
alpha-D-glucosamine 1-phosphate
Methanococcus maripaludis
Q6LYB4
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0.1
alpha-D-glucose 1-phosphate
Methanococcus maripaludis
Q6LYB4
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2.42 - 7.9
D-Glucosamine 6-phosphate
0.0055 - 0.0138
D-glucose 1-phosphate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.007
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substrate: D-glucose 6-phosphate
0.06
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substrate: D-glucose 1-phosphate
0.55
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substrate: D-mannose 1-phosphate
2.5
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substrate: D-glucosamine 6-phosphate
3
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6x His-tagged recombinant enzyme
10
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substrate: D-glucosamine 6-phosphate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
strain BL23 does not produce exopolysaccharides, therefore it might be a suitable host for the production of oligosaccharides
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48370
calculated from amino acid sequence
93100
dynamic light scattering
340000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
2 * 51000, X-ray crystallography
trimer
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3 * 47412, gel filtration, mass spectrometry
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the crystal structure of Bacillus anthracis phosphoglucosamine mutase is determined to a resolution of 2.7 A
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
near homogeneity
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near homogeneity, recombinant enzyme
near homogeneity; near homogeneity, recombinant enzyme
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Ni+ affinity column chromatography
to homogeneity, recombinant enzyme
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using His-Select Ni-Affinity gel
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 Star (DE3) cells
expressed in Escherichia coli BL21(DE3) cells
gene glmM, DNA and amino acid sequence determination and analysis, transcriptional and expression analysis, recombinant overexpression in Lactobacillus casei BL23 leading to a 6.43fold increased enzyme activity
gene glmM, subcloning in Escherichia coli strain NOvaBlue
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into the pDONR221 vector and subsequently into the pDEST17 vector for expression in Escherichia coli BL21DE3 cells
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into the pFW5 (Spec_r) Escherichia coli - streptococcus shuttle plasmid to create the mutant glmM gene, into the shuttle vector pDL289 to complement the glmM-deficient mutant strain
overexpression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
a glmM-deficient Streptococcus mutans strain is used
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S100T
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contributes to the specificity towards sugar- or aminosugar-phosphates, much more efficient in catalysis of the phosphoglucose mutase reaction
glmM mutant
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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