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 hide
2.7.1.59
-
RECOMMENDED NAME
GeneOntology No.
N-acetylglucosamine kinase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + N-acetyl-D-glucosamine = ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Amino sugar and nucleotide sugar metabolism
-
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chitin derivatives degradation
-
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Metabolic pathways
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N-acetylglucosamine degradation II
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SYSTEMATIC NAME
IUBMB Comments
ATP:N-acetyl-D-glucosamine 6-phosphotransferase
The bacterial enzyme also acts on D-glucose.
CAS REGISTRY NUMBER
COMMENTARY hide
9027-48-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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-
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Manually annotated by BRENDA team
gene murK
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-
Manually annotated by BRENDA team
no activity in Saccharomyces cerevisiae
-
-
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Manually annotated by BRENDA team
malaria parasite
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Manually annotated by BRENDA team
strain 523 serotype 14
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Manually annotated by BRENDA team
strain 523 serotype 14
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Manually annotated by BRENDA team
hog
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
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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
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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
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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-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-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
show the reaction diagram
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
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30% of the activity with ATP
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-
?
ITP + N-acetyl-D-glucosamine
IDP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
75% of the activity with ATP
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-
?
N-acetylglucosamine + ATP
N-acetylglucosamine 6-phosphate + ADP
show the reaction diagram
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predominantely beta-N-acetylglucosamine 6-phosphate
-
?
N-butylglucosamine + ATP
?
show the reaction diagram
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-
-
-
?
additional information
?
-
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-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ba2+
-
can partially replace Mg2+ in activation
Ca2+
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can partially replace Mg2+ in activation
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoic acid)
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substrates partially protect against inactivation
arsenite/2,3-dimercaptopropanol
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substrates partially protect against inactivation
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D-glucosamine
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D-glucose
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competitive with N-acetyl-D-glucosamine
Diamide
-
substrates partially protect against inactivation
diphosphate
-
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EDTA
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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
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substrates partially protect against inactivation
N-acetyl-D-glucosamine
N-acetyl-D-glucosamine 6-phosphate
N-acetyl-D-glucosamine-6-phosphate
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non-competitive
N-acetyl-D-mannosamine
N-ethylmaleimide
N-Methyl-D-glucosamine
-
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p-chloromercuribenzoate
p-hydroxymercuribenzoate
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no protection by substrate, protection but not reversal of inhibition by thioethanol, complete inhibition above 0.00125 mM, cysteine reverses inhibition
Periodate
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substrates partially protect against inactivation
phosphate
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UDP-N-acetylglucosamine
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2- mercaptoethanol
cysteine
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00014 - 1.82
ATP
0.0011 - 600
D-glucose
0.426
D-mannose
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37C, pH 7.5
0.00025
ITP
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37C, pH 7.8
0.1 - 0.23
MgATP2-
0.00005 - 1.33
N-acetyl-D-glucosamine
0.95 - 1
N-acetyl-D-mannosamine
additional information
additional information
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Km for both substrates tested for wild type and all mutant enzymes
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03 - 65
N-acetyl-D-glucosamine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
510.2
N-acetyl-D-glucosamine
Clostridium acetobutylicum
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pH 7.5, 37C
300
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.9
ADP
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37C, pH 9.0
0.01
D-glucosamine
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37C, pH 7.8
0.0018
D-glucose
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for reaction with N-acetyl-D-glucosamine, 30C, pH 7.4
0.0009
N-acetyl-D-glucosamine
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for reaction with glucose, 30C, pH 7.4
0.001
N-Methyl-D-glucosamine
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37C, pH 7.8
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00009
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37C, pH 7.5
0.00012
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37C, pH 7.5
0.009
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spleen, 37C, pH 9.0
0.0183
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wild-type cell extract
0.025
-
spleen, 37C, pH 9.0
0.137
enzyme expressed in E. coli, 37C, pH 7.5
1.28
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purified enzyme, 37C, pH 8.0
4.6
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purified enzyme, 37C, pH 7.8
9.5
-
purified enzyme, 30C, pH 7.6
25
purified enzyme from E. coli, 37C, pH 7.5
33.3
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purified native enzyme
39
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purified enzyme from liver, 32C, pH 7.5
42
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purified enzyme from kidney, 32C, pH 7.5
52.4
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purified enzyme, 37C, pH 7.5
90
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purified enzyme, 37C, pH 9.5
250
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purified enzyme, 30C, pH 7.4
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 9.5
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7.8
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assay at
7.8 - 8
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8.6 - 9.4
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 10.5
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half maximal activity at about pH 6.5 and pH 10.5, inactive at pH 5.0 and below
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Vibrio vulnificus (strain CMCP6)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41000
SDS-PAGE, from E. coli
42000
-
SDS-PAGE, from E. coli
75000
-
gel filtration
77000
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gel filtration
80000
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gel filtration
373000
calculated from DNA sequence
374000
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calculated from DNA sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 34329, sequence calculation
homodimer
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x-ray crystallography
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in 100 mM HEPES (pH 7.0), 100 mM NaCl, 8% (w/v) PEG 4000 and 2 mM N-acetyl-D-glucosamine
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
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50% loss of activity within 2 min, no protection with added substrate
641694
6.2 - 8.5
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relatively stable at pH 6.2, rapid loss of activity above pH 8.5
641697
9.5
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no loss of activity within 30 min at 30C
641692
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
at 30C, the purified protein loses activity within hours of incubation, regardless of the addition of protease inhibitors
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate partially stabilizes against temperature inactivation
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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
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stable to dialysis
substrate at 0.2 M stabilizes, unstable in absence of substrate at 4C
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unstable to dialysis and gel filtration, 0.013 mM substrate protects against inactivation
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unstable to freezing and thawing, heat and low pH
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-10C, several months, no loss of activity
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-20C, stable for at least 6 months
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-20C, stable for several months
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-25C, stable for several months
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-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
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0-2C, 20 mM potassium phosphate, pH 7.6, 1 mM EDTA, 10 mM 2-mercaptoethanol, stable for at least 1 week
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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
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4C, stable for at least 3 days
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
from E. coli
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from liver and kidney
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fusion protein from Escherichia coli
glutathione Sepharose column chromatography, MonoQ HR 5/5 column chromatography, and Superdex75 gel filtration
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native enzyme 842fold from K12 strain MG1655 in a multistep procedure, recombinant enzyme from strain XL1-Blue
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recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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recombinnat TAP- and His-tagged HXK1 by tandem affinity purification using anti-FLAG and Ni-nitrilotriacetic acid agarose
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
6 point mutations in cysteine residues, expression in Escherichia coli BL21
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DNA and amino acid sequence determination and analysis, overexpression in strain XL1-Blue
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expressed in Escherichia coli strain BL21 (DE3)
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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
expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
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functionally expressed in Escherichia coli as glutathione-S-transferase fusion protein, active enzyme
functionally expressed in Escherichia coli BL21, active enzyme, high rate of protein expression in transfected cells, inclusion bodies
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
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GST fusion protein, expressed in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
HXK1 expression levels are upregulated in filamentation inducing media
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C131S
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strongly decreased activity, very low affinity for N-acetyl-D-glucosamine
C143S
-
strongly decreased activity, very low affinity for ATP
C211S
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slightly decreased activity
C217S
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decreased activity, low affinity for N-acetyl-D-glucosamine
C268S
-
decreased activity
C45S
-
very slightly decreased activity, no function in substrate binding
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
the kinase is applied for high-sensitive detection of the amino sugars in cell wall preparations by radioactive phosphorylation
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