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Information on EC 2.7.1.59 - N-acetylglucosamine kinase and Organism(s) Mus musculus and UniProt Accession Q9QZ08

for references in articles please use BRENDA:EC2.7.1.59
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EC Tree
IUBMB Comments
The bacterial enzyme also acts on D-glucose.
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This record set is specific for:
Mus musculus
UNIPROT: Q9QZ08
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
n-acetylglucosamine kinase, glcnac kinase, n-acetyl-d-glucosamine kinase, canag5p, glcnac-kinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N-acetyl-D-glucosamine kinase
-
2-acetylamino-2-deoxy-D-glucose kinase
-
-
-
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acetylaminodeoxyglucokinase
-
-
-
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acetylglucosamine kinase(phosphorylating)
-
-
-
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ATP:2-acetylamino-2-deoxy-D-glucose 6-phosphotransferase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
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
-
SUBSTRATE
PRODUCT                       
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
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
show the reaction diagram
recombinant enzyme, same rate as with N-acetyl-D-glucosamine
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
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
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
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
N-acetyl-D-glucosamine
inhibition of activity with N-acetyl-D-mannosamine
N-acetyl-D-mannosamine
no inhibition of activity with N-acetyl-D-glucosamine
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
Km for both substrates tested for wild type and all mutant enzymes
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.137
enzyme expressed in E. coli, 37°C, pH 7.5
25
purified enzyme from E. coli, 37°C, pH 7.5
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme promotes dynein functionality by interacting with dynein light chain roadblock type 1 and efficiently suppressing mutant huntingtin Q74 and alpha-synuclein A53T aggregation in mouse brain cells
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NAGK_MOUSE
343
0
37268
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
373000
calculated from DNA sequence
41000
SDS-PAGE, from E. coli
39000
-
SDS-PAGE, wild type protein
42000
-
SDS-PAGE, from E. coli
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 37000, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D107A
inactive
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
from E. coli
from E. coli
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
functionally expressed in Escherichia coli BL21, active enzyme, high rate of protein expression in transfected cells, inclusion bodies
6 point mutations in cysteine residues, expression in Escherichia coli BL21
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hinderlich, S.; Berger, M.; Schwarzkopf, M.; Effertz, K.; Reutter, W.
Molecular cloning and characterization of murine and human N-acetylglucosamine kinase
Eur. J. Biochem.
267
3301-3308
2000
Mus musculus (Q9QZ08), Mus musculus, Homo sapiens (Q9UJ70), Homo sapiens
Manually annotated by BRENDA team
Berger, M.; Chen, H.; Reutter, W.; Hinderlich, S.
Structure and function of N-acetylglucosamine kinase. Identification of two active site cysteines
Eur. J. Biochem.
269
4212-4218
2002
Mus musculus
Manually annotated by BRENDA team
Ripon, M.K.H.; Lee, H.; Dash, R.; Choi, H.J.; Oktaviani, D.F.; Moon, I.S.; Haque, M.N.
N-acetyl-D-glucosamine kinase binds dynein light chain roadblock 1 and promotes protein aggregate clearance
Cell Death Dis.
11
619
2020
Mus musculus (Q9QZ08), Mus musculus
Manually annotated by BRENDA team