Information on EC 2.7.1.59 - N-acetylglucosamine kinase

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

EC NUMBER
COMMENTARY
2.7.1.59
-
RECOMMENDED NAME
GeneOntology No.
N-acetylglucosamine kinase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ATP + N-acetyl-D-glucosamine = ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Amino sugar and nucleotide sugar metabolism
-
Biosynthesis of secondary metabolites
-
chitin derivatives degradation
-
N-acetylglucosamine degradation II
-
SYSTEMATIC NAME
IUBMB Comments
ATP:N-acetyl-D-glucosamine 6-phosphotransferase
The bacterial enzyme also acts on D-glucose.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2-acetylamino-2-deoxy-D-glucose kinase
-
-
-
-
acetylaminodeoxyglucokinase
-
-
-
-
acetylglucosamine kinase(phosphorylating)
-
-
-
-
ATP:2-acetylamino-2-deoxy-D-glucose 6-phosphotransferase
-
-
-
-
CaNag5p
-
part of cluster with 6 genes, product from gene CaNag5
GlcNAc kinase
Q59RG5
-
GlcNAc kinase
-
-
GlcNAc kinase
Q9UJ70
-
Hxk1
Q59RG5
-
N-acetyl-D-glucosamine kinase
-
-
N-acetylglucosamine kinase
Q9UJ70
-
N-acetylmuramic acid/N-acetylglucosamine kinase
-
-
NAG5
Q59RG5
-
CAS REGISTRY NUMBER
COMMENTARY
9027-48-9
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
gene hxk1
-
-
Manually annotated by BRENDA team
gene nagK
-
-
Manually annotated by BRENDA team
sequence with additional 92 bp sequence found in lung, EMBL: AF242911
SwissProt
Manually annotated by BRENDA team
no activity in Saccharomyces cerevisiae
-
-
-
Manually annotated by BRENDA team
malaria parasite
-
-
Manually annotated by BRENDA team
strain 523 serotype 14
-
-
Manually annotated by BRENDA team
Streptococcus pyogenes 523
strain 523 serotype 14
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
evolution
-
the enzyme is a member of the BcrAD/BadFGlike ATPase family
malfunction
-
the homozygous hxk1 mutant H8-1-103 is constitutively filamentous and hyperfilamentous under filamentation inducing conditions
metabolism
-
HXK1 acts as both positive and negative regulator of transcription of genes involved in maintaining cellular homeostasis, regulatory mechanism involved in filamentation repression, overview
physiological function
-
HXK1 plays a crucial role in morphogenesis, GlcNAc signaling/metabolic genes expression and maintenance of various cellular functions in Candida albicans, Hxk1 is involved in the cell wall synthesis and in repression of hyphal specific genes in addition to metabolic genes. Its regulation of filamentation and GlcNAc metabolism is independent of the known classical regulators like EFG1, CPH1, RAS1, TPK2 or TUP1, regulatory mechanism involved in filamentation repression, overview
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-O-methyl-beta-N-acetyl-glucosamine + ATP
?
show the reaction diagram
-
-
-
-
?
3,4-di-O-methyl-beta-N-acetyl-D-glucosamine + ATP
?
show the reaction diagram
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
very poor substrate, 4.5% of the rate with N-acetyl-D-glucosamine
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
15% of the rate with N-acetyl-D-glucosamine
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
at equal rate than N-acetyl-D-glucosamine
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
21% of the activity with N-acetyl-D-glucosamine
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
Streptococcus pyogenes 523
-
at equal rate than N-acetyl-D-glucosamine
-
?
ATP + D-mannose
?
show the reaction diagram
-
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-, Q9QZ08
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
Q9UJ70
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
Q59RG5
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
highly specific
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
highly specific
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
first enzyme of N-acetyl-D-glucosamine salvage pathway
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
first reaction of inducible N-acetylglucosamine catabolic pathway, enables organism to grow on N-acetylglucosamine as sole carbon source
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
first reaction of inducible N-acetylglucosamine catabolic pathway, enables organism to grow on N-acetylglucosamine as sole carbon source
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
part of glycoprotein synthesis pathway
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
involved in UDP-N-acetylglucosamine formation
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
enzyme is important in cell wall murein recycling, 60% of the the murein of the side wall is degraded
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
Streptococcus pyogenes 523
-
-
-
?
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
show the reaction diagram
-
-
-
-
-
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
show the reaction diagram
-
roughly 50% of activity
-
-
?
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
show the reaction diagram
-
roughly 50% of activity
-
-
?
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
show the reaction diagram
-, Q9QZ08
recombinant enzyme, same rate as with N-acetyl-D-glucosamine
-
-
?
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
show the reaction diagram
-
78% of the rate with N-acetyl-D-glucosamine
-
-
?
CTP + N-acetyl-D-glucosamine
CDP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
?
dATP + N-acetyl-D-glucosamine
dADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
?
GTP + N-acetyl-D-glucosamine
GDP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
30% of the activity with ATP
-
-
?
N-acetylglucosamine + ATP
N-acetylglucosamine 6-phosphate + ADP
show the reaction diagram
-
-
predominantely beta-N-acetylglucosamine 6-phosphate
-
?
N-butylglucosamine + ATP
?
show the reaction diagram
-
-
-
-
?
ITP + N-acetyl-D-glucosamine
IDP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
75% of the activity with ATP
-
-
?
additional information
?
-
-, Q9QZ08
D-fructose, D-mannose, D-maltose, D-galactose, N-acetyl-D-galactosamine, ribose, fucose do not serve as substrates
-
-
-
additional information
?
-
-
D-fructose, D-mannose, D-maltose, D-galactose, N-acetyl-D-galactosamine, N-acetyl-D-mannosamine do not serve as substrates
-
-
-
additional information
?
-
-
D-fructose, D-mannose, D-maltose, D-galactose, N-acetyl-D-galactosamine, N-acetyl-D-mannosamine do not serve as substrates
-
-
-
additional information
?
-
-
no activity with UTP, CTP, ADP or phosphoenol pyruvate
-
-
-
additional information
?
-
-
N-methyl-D-glucosamine, D-glucosamine, N-acetyl-D-galactosamine, N-acetyl-D-mannosamine do not serve as substrates, very low activities with UTP, GTP and CTP
-
-
-
additional information
?
-
-
no activity with D-galactose and D-fructose, very low activities with N-acetyl-D-galactosamine: 7.6%, D-glucosamine: 11.2%, D-mannosamine: 2.7%, D-galactosamine: 2.1%, D-mannose: 4.5% and D-xylose: 2.1%
-
-
-
additional information
?
-
-
D-fructose, D-galactose, galactosamine, N-acetyl-D-galactosamine, mannosamine, N-acetyl-D-mannosamine do not serve as substrates
-
-
-
additional information
?
-
-
poor activity with mannose, galactose, glucosamine, D-mannosamine, N-acetylmannosamine, and N-acetylgalactosamine
-
-
-
additional information
?
-
-
interaction of HXK1 with histone deacetylase SIR2 under filamentation inducing conditions
-
-
-
additional information
?
-
-
the enzyme has a unique specificity for both amino sugars of the bacterial cell wall, N-acetylmuramic acid and N-acetylglucosamine, which are phosphorylated at the 6-hydroxyl group, see also EC 2.7.1.170, the kcat value is 1.5fold higher for the latter substrate. Neither the non-N-acetylated forms of the cell wall sugars, i.e., glucosamine and/or muramic acid, nor epimeric hexoses or 1,6-anhydro-MurNAc are substrates for the enzyme. Product identificsation by nonradioactive and radioactive TLC
-
-
-
additional information
?
-
Streptococcus pyogenes 523
-
D-fructose, D-mannose, D-maltose, D-galactose, N-acetyl-D-galactosamine, N-acetyl-D-mannosamine do not serve as substrates
-
-
-
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
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-, Q9QZ08
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
Q9UJ70
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
Q59RG5
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
first enzyme of N-acetyl-D-glucosamine salvage pathway
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
first reaction of inducible N-acetylglucosamine catabolic pathway, enables organism to grow on N-acetylglucosamine as sole carbon source
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
first reaction of inducible N-acetylglucosamine catabolic pathway, enables organism to grow on N-acetylglucosamine as sole carbon source
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
part of glycoprotein synthesis pathway
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
involved in UDP-N-acetylglucosamine formation
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
enzyme is important in cell wall murein recycling, 60% of the the murein of the side wall is degraded
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
Streptococcus pyogenes 523
-
-
-
?
additional information
?
-
-
interaction of HXK1 with histone deacetylase SIR2 under filamentation inducing conditions
-
-
-
additional information
?
-
-
the enzyme has a unique specificity for both amino sugars of the bacterial cell wall, N-acetylmuramic acid and N-acetylglucosamine, which are phosphorylated at the 6-hydroxyl group, see also EC 2.7.1.170, the kcat value is 1.5fold higher for the latter substrate. Neither the non-N-acetylated forms of the cell wall sugars, i.e., glucosamine and/or muramic acid, nor epimeric hexoses or 1,6-anhydro-MurNAc are substrates for the enzyme. Product identificsation by nonradioactive and radioactive TLC
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ba2+
-
can partially replace Mg2+ in activation
Ca2+
-
can partially replace Mg2+ in activation
Co2+
-
can partially replace Mg2+ in activation
Co2+
-
can partially replace Mg2+ in activation
Co2+
-
can partially replace Mg2+ in activation
Mg2+
-
required
Mg2+
-
required
Mg2+
-
required
Mg2+
-
required
Mn2+
-
can partially replace Mg2+ in activation
Mn2+
-
can partially replace Mg2+ in activation
Mn2+
-
can partially replace Mg2+ in activation
additional information
-
slight activities with Ni2+, Zn2+, Cu2+
additional information
-
no activity with Ca2+, Ba2+
additional information
-
Mg2+ is not essential for activity
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoic acid)
-
substrates partially protect against inactivation
ADP
-
strong competitive inhibitor
ADP
-
strong competitive inhibitor
arsenite/2,3-dimercaptopropanol
-
substrates partially protect against inactivation
-
D-glucosamine
-
-
D-glucose
-
competitive with N-acetyl-D-glucosamine
Diamide
-
substrates partially protect against inactivation
diphosphate
-
-
EDTA
-
a 3fold excess of EDTA compared to the Mg2+ concentration strongly represses the MurK activity. Addition of 2 mM MgCl2 to the reaction mixture partially restores MurK activity
iodoacetamide
-
substrates partially protect against inactivation
N-acetyl-D-glucosamine
-
competitive with glucose
N-acetyl-D-glucosamine
-
inhibits phosphorylation of D-glucose
N-acetyl-D-glucosamine
-, Q9QZ08
inhibition of activity with N-acetyl-D-mannosamine
N-acetyl-D-glucosamine 6-phosphate
-
-
N-acetyl-D-glucosamine-6-phosphate
-
non-competitive
N-acetyl-D-mannosamine
-
inhibits phosphorylation of D-glucose
N-acetyl-D-mannosamine
-, Q9QZ08
no inhibition of activity with N-acetyl-D-glucosamine
N-ethylmaleimide
-
-
N-ethylmaleimide
-
substrates partially protect against inactivation
N-Methyl-D-glucosamine
-
-
p-chloromercuribenzoate
-
complete inhibition at 0.4 mM; reversible with cysteine or 2-mercaptoethanol
p-chloromercuribenzoate
-
irreversible
p-chloromercuribenzoate
-
reversible with cysteine or 2-mercaptoethanol
p-chloromercuribenzoate
-
-
p-hydroxymercuribenzoate
-
no protection by substrate, protection but not reversal of inhibition by thioethanol, complete inhibition above 0.00125 mM, cysteine reverses inhibition
Periodate
-
substrates partially protect against inactivation
UDP-N-acetylglucosamine
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2- mercaptoethanol
-
reverses inhibition with p-chloromercuribenzoate and loss of activity during storage
2- mercaptoethanol
-
-
cysteine
-
reverses inhibition with p-hydroxymercuribenzoate
cysteine
-
reverses inhibition with p-chloroxymercuribenzoate
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00014
-
ATP
-
37C, pH 7.8
0.9
-
ATP
-
pH 7.8, 37C
1.8
-
ATP
-
37C, pH 9.0
1.8
-
ATP
-
37C, pH 8.0
1.8
-
ATP
-
37C, pH 9.0
1.82
-
ATP
-
30C, pH 7.6
0.0011
-
D-glucose
-
30C, pH 7.4
0.005
-
D-glucose
-
37C, pH 7.8
0.483
-
D-glucose
-
37C, pH 7.5
37.2
-
D-glucose
-
pH 7.8, 37C
410
-
D-glucose
-
enzyme from kidney, 32C, pH 7.5
600
-
D-glucose
-
enzyme from liver, 32C, pH 7.5
0.426
-
D-mannose
-
37C, pH 7.5
0.00025
-
ITP
-
37C, pH 7.8
0.1
-
MgATP2-
-
enzyme from kidney with N-acetyl-D-glucosamine as substrate, 32C, pH 7.5
0.00005
-
N-acetyl-D-glucosamine
-
37C, pH 7.8
0.00077
-
N-acetyl-D-glucosamine
-
30C, pH 7.4
0.04
-
N-acetyl-D-glucosamine
-
enzyme from kidney, 32C, pH 7.5
0.05
-
N-acetyl-D-glucosamine
-
37C, pH 7.5
0.06
-
N-acetyl-D-glucosamine
-
enzyme from liver, 32C, pH 7.5
0.089
-
N-acetyl-D-glucosamine
-
37C, pH 7.5
0.11
-
N-acetyl-D-glucosamine
-
37C, pH 8.0
0.127
-
N-acetyl-D-glucosamine
-
pH 7.5, 37C
0.34
-
N-acetyl-D-glucosamine
-
pH 7.8, 37C
0.376
-
N-acetyl-D-glucosamine
-
37C, pH 7.5
0.445
-
N-acetyl-D-glucosamine
-
37C, pH 7.5
1.1
-
N-acetyl-D-glucosamine
-
37C, pH 9.0
1.33
-
N-acetyl-D-glucosamine
-
30C, pH 7.6
0.95
-
N-acetyl-D-mannosamine
-
enzyme from liver, 32C, pH 7.5
1
-
N-acetyl-D-mannosamine
-
enzyme from kidney, 32C, pH 7.5
1
-
N-acetyl-D-mannosamine
-
37C, pH 7.5
0.23
-
MgATP2-
-
enzyme from liver with N-acetyl-D-glucosamine as substrate, 32C, pH 7.5
additional information
-
additional information
-
Km for both substrates tested for wild type and all mutant enzymes
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.03
-
N-acetyl-D-glucosamine
-
37C, pH 7.5
0.0325
-
N-acetyl-D-glucosamine
-
37C, pH 7.5
65
-
N-acetyl-D-glucosamine
-
pH 7.5, 37C
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
510.2
-
N-acetyl-D-glucosamine
-
pH 7.5, 37C
13498
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.9
-
ADP
-
37C, pH 9.0
0.01
-
D-glucosamine
-
37C, pH 7.8
0.0018
-
D-glucose
-
for reaction with N-acetyl-D-glucosamine, 30C, pH 7.4
0.0009
-
N-acetyl-D-glucosamine
-
for reaction with glucose, 30C, pH 7.4
0.001
-
N-Methyl-D-glucosamine
-
37C, pH 7.8
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.00009
-
-
37C, pH 7.5
0.00012
-
-
37C, pH 7.5
0.009
-
-
spleen, 37C, pH 9.0
0.0183
-
-
wild-type cell extract
0.025
-
-
spleen, 37C, pH 9.0
0.137
-
-, Q9QZ08
enzyme expressed in E. coli, 37C, pH 7.5
1.28
-
-
purified enzyme, 37C, pH 8.0
4.6
-
-
purified enzyme, 37C, pH 7.8
9.5
-
-
purified enzyme, 30C, pH 7.6
25
-
-, Q9QZ08
purified enzyme from E. coli, 37C, pH 7.5
33.3
-
-
purified native enzyme
39
-
-
purified enzyme from liver, 32C, pH 7.5
42
-
-
purified enzyme from kidney, 32C, pH 7.5
52.4
-
-
purified enzyme, 37C, pH 7.5
90
-
-
purified enzyme, 37C, pH 9.5
250
-
-
purified enzyme, 30C, pH 7.4
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
8
-
strongly decreasing activity outside this range
7.5
9.5
-
-
7.8
8
-
-
7.8
-
-
assay at
8.6
9.4
-
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
10.5
-
half maximal activity at about pH 6.5 and pH 10.5, inactive at pH 5.0 and below
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
very high activity
Manually annotated by BRENDA team
Q9QZ08
very high activity
Manually annotated by BRENDA team
additional information
-
present in cancer cell lines
Manually annotated by BRENDA team
additional information
-
HXK1 expression levels are upregulated in filamentation inducing media, morphological and expression pattern analyses among wild type, hxk1 and different filamentation pathway mutants, overview
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Vibrio vulnificus (strain CMCP6)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
39000
-
-
SDS-PAGE, second band at 90000 Da shows no activity
39000
-
-
identification of 90000 Da band, found to be another protein; SDS-PAGE, second band at 90000 Da shows no activity
39000
-
-
SDS-PAGE, wild type protein
41000
-
-, Q9QZ08
SDS-PAGE, from E. coli
42000
-
-
SDS-PAGE, from E. coli
75000
-
-
gel filtration
77000
-
-
gel filtration
80000
-
-
gel filtration
373000
-
-, Q9QZ08
calculated from DNA sequence
374000
-
-
calculated from DNA sequence
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 34329, sequence calculation
dimer
-
postulated due to kinetic data
dimer
-
2 * 39000, SDS-PAGE, gel filtration
homodimer
-
x-ray crystallography
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
in 100 mM HEPES (pH 7.0), 100 mM NaCl, 8% (w/v) PEG 4000 and 2 mM N-acetyl-D-glucosamine
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
-
-
50% loss of activity within 2 min, no protection with added substrate
6.2
8.5
-
relatively stable at pH 6.2, rapid loss of activity above pH 8.5
9.5
-
-
no loss of activity within 30 min at 30C
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
at 30C, the purified protein loses activity within hours of incubation, regardless of the addition of protease inhibitors
60
-
-
25% loss of activity within 1 min in presence of 13% ammonium sulfate, stable for 1 h in presence of ammonium sulfate and substrate
60
-
-
84% loss of activity within 2 min, no protection with added substrate
65
-
-
heat treatment for 5 min included in purification procedure
65
-
-
complete inactivation with 2 min
70
-
-
complete inactivation with 1 min
70
-
-
complete inactivation with 2 min
70
-
-
50% loss of activity within 2 min
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
stable to dialysis
-
unstable to freezing and thawing, heat and low pH
-
unstable to dialysis and gel filtration, 0.013 mM substrate protects against inactivation
-
ammonium sulfate partially stabilizes against temperature inactivation
-
dialysis at 4C for 17 h against 0.005 M Tris buffer, pH 7.6, 92% loss of activity, 33% loss of activity in presence of 0.1 M N-acetyl-D-glucosamine or glucose, stable in presence of 0.2 M or 2.5
-
substrate at 0.2 M stabilizes, unstable in absence of substrate at 4C
-
stable to dialysis
-
unstable to freezing and thawing, heat and low pH
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
0-2C, 20 mM potassium phosphate, pH 7.6, 1 mM EDTA, 10 mM 2-mercaptoethanol, stable for at least 1 week
-
-20C, stable for several months
-
-80C, purified recombinant enzyme frozen in dry-ice/ethanol, fully stable for months, thawed samples retain full activity in 40% glycerol at -20C for a few months
-
-20C, stable for at least 6 months
-
4C, stable for at least 3 days
-
-10C, several months, no loss of activity
-
-25C, stable for several months
-
4C, 0.02 M potassium phosphate buffer, pH 7.6, 0.001 M EDTA, 0.01 M 2-mercaptoethanol, stable for at least a week
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
fusion protein from Escherichia coli
-
recombinnat TAP- and His-tagged HXK1 by tandem affinity purification using anti-FLAG and Ni-nitrilotriacetic acid agarose
-
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
native enzyme 842fold from K12 strain MG1655 in a multistep procedure, recombinant enzyme from strain XL1-Blue
-
fusion protein from Escherichia coli
-
glutathione Sepharose column chromatography, MonoQ HR 5/5 column chromatography, and Superdex75 gel filtration
-
from E. coli
-
from liver and kidney
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Saccharomyces cerevisiae strain BY4734 from the yeast PGK1 promoter leading to incorporation of exogenous GlcNAc into chitin in engineered Saccharomyces cerevisiae, which is devoid of GlcNAc kinase
Q59RG5
functionally expressed in Escherichia coli as glutathione-S-transferase fusion protein, active enzyme
-
gene hxk1, expression of GFP-tagged wild-type enzyme in enzyme-deficient disruption mutant Candida albicans strain CAI4 and expression of TAP- and His-tagged HXK1 under ADH1 p in CAI-4, co-expression with histone deacetylase SIR2
-
expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
-
DNA and amino acid sequence determination and analysis, overexpression in strain XL1-Blue
-
expressed in Escherichia coli strain BL21 (DE3)
-
functionally expressed in Escherichia coli as glutathione-S-transferase fusion protein, active enzyme
-
GST fusion protein, expressed in Escherichia coli
-
6 point mutations in cysteine residues, expression in Escherichia coli BL21
-
functionally expressed in Escherichia coli BL21, active enzyme, high rate of protein expression in transfected cells, inclusion bodies
-, Q9QZ08
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
HXK1 expression levels are upregulated in filamentation inducing media
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C131S
-
strongly decreased activity, very low affinity for N-acetyl-D-glucosamine
C143S
-
strongly decreased activity, very low affinity for ATP
C211S
-
slightly decreased activity
C217S
-
decreased activity, low affinity for N-acetyl-D-glucosamine
C268S
-
decreased activity
C45S
-
very slightly decreased activity, no function in substrate binding
additional information
Q59RG5
uptake of radiolabeled GlcNAc into Saccharomyces cerevisiae via native hexose transporters and its in vivo incorporation into GPI precursors and chitin, a long polymer of unbranched beta1,4-linked GlcNAc residues and is a critical structural component ofthe yeast cell wall, in cells heterologously expressing the enzyme, overview
additional information
-
construction of a homozygous hxk1 mutant H8-1-103
additional information
-
deletion mutants lack enzyme activity in the cytoplasm, but do not accumulate N-acetyl-D-glucosamine suggesting the existence of an alternative pathway for reutilization of N-acetyl-D-glucosamine, overview
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
analysis
-
the kinase is applied for high-sensitive detection of the amino sugars in cell wall preparations by radioactive phosphorylation