Information on EC 2.7.1.157 - N-acetylgalactosamine kinase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.7.1.157
-
RECOMMENDED NAME
GeneOntology No.
N-acetylgalactosamine kinase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + N-acetyl-alpha-D-galactosamine = ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:N-acetyl-D-galactosamine 1-phosphotransferase
The enzyme is highly specific for GalNAc as substrate, but has slight activity with D-galactose [2]. Requires Mg2+, Mn2+ or Co2+ for activity, with Mg2+ resulting in by far the greatest stimulation of enzyme activity.
CAS REGISTRY NUMBER
COMMENTARY hide
180984-03-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-phosphate + N-acetyl-alpha-D-galactosamine
acetate + N-acetyl-alpha-D-galactosamine 1-phosphate
show the reaction diagram
-
8% of the specific activity with ATP
-
-
?
ATP + D-galactose
ADP + D-galactose 1-phosphate
show the reaction diagram
ATP + N-acetyl-alpha-D-galactosamine
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
show the reaction diagram
ATP + N-acetyl-alpha-D-glucosamine
ADP + N-acetyl-alpha-D-glucosamine 1-phosphate
show the reaction diagram
-
-
-
-
?
ATP + N-acetyl-alpha-D-mannosamine
ADP + N-acetyl-alpha-D-mannosamine 1-phosphate
show the reaction diagram
-
-
-
-
?
ATP + N-acetyl-D-galactosamine
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
show the reaction diagram
ITP + N-acetyl-alpha-D-galactosamine
IDP + N-acetyl-alpha-D-galactosamine 1-phosphate
show the reaction diagram
-
9% of the specific activity with ATP
-
-
?
phosphoenolpyruvate + N-acetyl-alpha-D-galactosamine
pyruvate + N-acetyl-alpha-D-galactosamine 1-phosphate
show the reaction diagram
-
11% of the specific activity with ATP
-
-
?
additional information
?
-
ordered ternary complex mechanism in which ATP is the first substrate to bind
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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
ATP + N-acetyl-alpha-D-galactosamine
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
show the reaction diagram
-
the enzyme is involved in a salvage pathway for reutilization of free GalNAc derived from the degradation of complex carbohydrates
-
-
?
ATP + N-acetyl-D-galactosamine
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
divalent cation required, efficiency in descending order: Mg2+ > Mn2+ > Co2+, optimum Co2+ concentration is 10 mM, maximal activity is 50% of that with Mg2+
Mn2+
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divalent cation required, efficiency in descending order: Mg2+ > Mn2+ > Co2+, optimum Mn2+ concentration is 2-8 mM, maximal activity is 50% of that with Mg2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
alpha-methylgalactopyranoside
-
uncompetitive inhibition with respect to ATP; uncompetitive with respect to ATP, poor inhibitor
N-acetyl-D-galactosamine
-
substrate inhibition
N-acetylgalactosamine
-
substrate inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.006 - 0.13
ATP
0.5
D-galactose
-
-
0.5
galactose
-
-
0.04 - 0.95
N-acetyl-alpha-D-galactosamine
0.051 - 0.39
N-acetyl-alpha-D-glucosamine
0.25 - 4.1
N-acetyl-alpha-D-mannosamine
0.04 - 0.14
N-acetyl-D-galactosamine
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1 - 2.5
ATP
0.62 - 3.2
N-acetyl-alpha-D-galactosamine
0.063 - 0.18
N-acetyl-alpha-D-glucosamine
0.053 - 0.4
N-acetyl-alpha-D-mannosamine
1 - 2.5
N-acetyl-D-galactosamine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
13
N-acetylgalactosamine
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pH 8.0, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.43
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
assay at
8.5 - 9
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-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.8 - 11
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-
6 - 10
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pH 6.0: about 45% of maximal activity, pH 10.0: about 35% of maximal activity
7 - 8
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additional information
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pH dependency of the reaction mechanism, overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
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-
Manually annotated by BRENDA team
additional information
-
no activity in pancreas, brain, aorta, heart
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
57000
-
x * 57000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 50000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, structure auf enzyme solved in presence of Mn-5'-adenylyl-beta,gamma-imidodiphosphate and GalNAc or MgATP and GalNAc (which results in bound products in the active site)
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 0.5 mg/ml in a buffered (pH 7.5) solution containing 30% glycerol, no loss of activity after one year
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant GALK2 from Escherichia coli
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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expression in Escherichia coli; GALK2, functional expression in Escherichia coli
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expression in Saccharomyce cerevisiae
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F444A
-
mutation in residue equivalent to residue Tyr379 of galactokinase, whose alteration dramatically enhances the substrate range of this enzyme. Mutation does not result in large changes to the specificity of the enzyme
F444C
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mutation in residue equivalent to residue Tyr379 of galactokinase, whose alteration dramatically enhances the substrate range of this enzyme. Mutation does not result in large changes to the specificity of the enzyme but increases turnover rate with N-acetylgalactosamine
F444H
-
mutation in residue equivalent to residue Tyr379 of galactokinase, whose alteration dramatically enhances the substrate range of this enzyme. Mutation does not result in large changes to the specificity of the enzyme
F444K
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mutation in residue equivalent to residue Tyr379 of galactokinase, whose alteration dramatically enhances the substrate range of this enzyme. Mutation does not result in large changes to the specificity of the enzyme
F444R
-
mutation in residue equivalent to residue Tyr379 of galactokinase, whose alteration dramatically enhances the substrate range of this enzyme. Mutation does not result in large changes to the specificity of the enzyme
F444S
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mutation in residue equivalent to residue Tyr379 of galactokinase, whose alteration dramatically enhances the substrate range of this enzyme. Mutation does not result in large changes to the specificity of the enzyme but increases turnover rate with N-acetylgalactosamine
F444W
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mutation in residue equivalent to residue Tyr379 of galactokinase, whose alteration dramatically enhances the substrate range of this enzyme. Mutation does not result in large changes to the specificity of the enzyme
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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synthesis of UDP-GalNAc with high yield from GalNAc, UTP and ATP using recombinant human GalNAc kinase GK2 and UDP-GalNAc pyrophosphorylase AGX1