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Information on EC 2.7.1.157 - N-acetylgalactosamine kinase and Organism(s) Homo sapiens and UniProt Accession Q01415
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2.7.1.157 N-acetylgalactosamine kinaseIUBMB Comments
The enzyme is highly specific for GalNAc as substrate, but has slight activity with D-galactose . Requires Mg2+, Mn2+ or Co2+ for activity, with Mg2+ resulting in by far the greatest stimulation of enzyme activity.
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Word Map
- 2.7.1.157
- galactokinase
- galactose
-
nalidixic
-
antimutator
-
proofreading
-
gale
-
papillation
- mgatp
- udp-galnac
- udp-galactose
- synthesis
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
galk2, galnac kinase, n-acetylgalactosamine kinase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + N-acetyl-alpha-D-galactosamine = ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
ATP hydrolysis and methanolysis reaction pathways, overview
-
ATP + N-acetyl-alpha-D-galactosamine = ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
ordered ternary complex reaction mechanism, in which ATP binds first, overview. Ionizable residues play a role in substrate binding and catalysis
PATHWAY SOURCE
PATHWAYS
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
180984-03-6
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + N-acetyl-alpha-D-glucosamine
ADP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
ATP + N-acetyl-alpha-D-mannosamine
ADP + N-acetyl-alpha-D-mannosamine 1-phosphate
-
-
-
?
ATP + D-galactose
ADP + D-galactose 1-phosphate
-
phosphorylation of galactose at millimolar concentrations
-
-
?
ATP + N-acetyl-alpha-D-galactosamine
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
-
?
ATP + N-acetyl-alpha-D-galactosamine
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
-
-
?
ATP + N-acetyl-alpha-D-galactosamine
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
-
-
?
ATP + N-acetyl-alpha-D-galactosamine
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
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
-
-
-
-
?
ATP + N-acetyl-D-galactosamine
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
-
?
additional information
?
-
-
ordered ternary complex mechanism in which ATP is the first substrate to bind
-
-
?
additional information
?
-
ordered ternary complex mechanism in which ATP is the first substrate to bind
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + N-acetyl-alpha-D-galactosamine
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
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
-
-
-
-
?
ATP + N-acetyl-D-galactosamine
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
-
addition of Mg2+ leads to partly compensating changes in DELTAH and TDELTAS, accelerating the nonenzymatic methanolysis of ATP 11fold. ATP hydrolysis and methanolysis reaction pathways, overview
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
-
addition of Mg2+ leads to partly compensating changes in DELTAH and TDELTAS, accelerating the nonenzymatic methanolysis of ATP 11fold
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
alpha-methylgalactopyranoside
uncompetitive with respect to ATP, poor inhibitor
alpha-methylgalactopyranoside
uncompetitive inhibition with respect to ATP
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.006
ATP
mutant F444A, 37°C, pH 7.5, cosubstrate N-acetyl-alpha-D-galactosamine
0.009
ATP
mutant F444R, 37°C, pH 7.5, cosubstrate N-acetyl-alpha-D-galactosamine
0.009
ATP
wild-type, 37°C, pH 7.5, cosubstrate N-acetyl-alpha-D-glucosamine
0.011
ATP
mutant F444H, 37°C, pH 7.5, cosubstrate N-acetyl-alpha-D-galactosamine
0.013
ATP
mutant F444H, 37°C, pH 7.5, cosubstrate N-acetyl-alpha-D-glucosamine
0.013
ATP
mutant F444S, 37°C, pH 7.5, cosubstrate N-acetyl-alpha-D-glucosamine
0.015
ATP
mutant F444K, 37°C, pH 7.5, cosubstrate N-acetyl-alpha-D-galactosamine
0.015
ATP
mutant F444K, 37°C, pH 7.5, cosubstrate N-acetyl-alpha-D-glucosamine
0.015
ATP
mutant F444R, 37°C, pH 7.5, cosubstrate N-acetyl-alpha-D-glucosamine
0.017
ATP
mutant F444C, 37°C, pH 7.5, cosubstrate N-acetyl-alpha-D-mannosamine
0.017
ATP
mutant F444H, 37°C, pH 7.5, cosubstrate N-acetyl-alpha-D-mannosamine
0.018
ATP
mutant F444C, 37°C, pH 7.5, cosubstrate N-acetyl-alpha-D-glucosamine
0.018
ATP
wild-type, 37°C, pH 7.5, cosubstrate N-acetyl-alpha-D-galactosamine
0.019
ATP
mutant F444S, 37°C, pH 7.5, cosubstrate N-acetyl-alpha-D-galactosamine
0.024
ATP
mutant F444R, 37°C, pH 7.5, cosubstrate N-acetyl-alpha-D-mannosamine
0.024
ATP
mutant F444W, 37°C, pH 7.5, cosubstrate N-acetyl-alpha-D-galactosamine
0.025
ATP
mutant F444A, 37°C, pH 7.5, cosubstrate N-acetyl-alpha-D-glucosamine
0.027
ATP
mutant F444C, 37°C, pH 7.5, cosubstrate N-acetyl-alpha-D-galactosamine
0.028
ATP
mutant F444K, 37°C, pH 7.5, cosubstrate N-acetyl-alpha-D-mannosamine
0.032
ATP
wild-type, 37°C, pH 7.5, cosubstrate N-acetyl-alpha-D-mannosamine
0.039
ATP
mutant F444A, 37°C, pH 7.5, cosubstrate N-acetyl-alpha-D-mannosamine
0.13
ATP
mutant F444S, 37°C, pH 7.5, cosubstrate N-acetyl-alpha-D-mannosamine
additional information
additional information
-
enzyme kinetics and thermodynamics, detailed overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GALK2_HUMAN
458
0
50378
Swiss-Prot
Mitochondrion (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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)
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
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
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
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
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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 0.5 mg/ml in a buffered (pH 7.5) solution containing 30% glycerol, no loss of activity after one year
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
-
synthesis of UDP-GalNAc with high yield from GalNAc, UTP and ATP using recombinant human GalNAc kinase GK2 and UDP-GalNAc pyrophosphorylase AGX1
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pastuszak, I.; Drake, R.; Elbein, A.D.
Kidney N-acetylgalactosamine (GalNAc)-1-phosphate kinase, a new pathway of GalNAc activation
J. Biol. Chem.
271
20776-20782
1996
Homo sapiens, Oryctolagus cuniculus, Sus scrofa
Pastuszak, I.; O'Donnell, J.; Elbein, A.D.
Identification of the GalNAc kinase amino acid sequence
J. Biol. Chem.
271
23653-23656
1996
Homo sapiens, Sus scrofa
Thoden, J.B.; Holden, H.M.
The molecular architecture of human N-acetylgalactosamine kinase
J. Biol. Chem.
280
32784-32791
2005
Homo sapiens
Bourgeaux, V.; Piller, F.; Piller, V.
Two-step enzymatic synthesis of UDP-N-acetylgalactosamine
Bioorg. Med. Chem. Lett.
15
5459-5462
2005
Homo sapiens
Stockbridge, R.B.; Wolfenden, R.
The intrinsic reactivity of ATP and the catalytic proficiencies of kinases acting on glucose, N-acetylgalactosamine, and homoserine: a thermodynamic analysis
J. Biol. Chem.
284
22747-22757
2009
Homo sapiens
Agnew, A.; Timson, D.
Mechanistic studies on human N-acetylgalactosamine kinase
J. Enzyme Inhib. Med. Chem.
25
370-376
2009
Homo sapiens, Homo sapiens (Q01415)
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