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Information on EC 2.7.1.59 - N-acetylglucosamine kinase and Organism(s) Homo sapiens
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2.7.1.59 N-acetylglucosamine kinaseIUBMB Comments
The bacterial enzyme also acts on D-glucose.
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Word Map
- 2.7.1.59
- albicans
- n-acetylmannosamine
- hexokinases
-
glcnac-6-phosphate
- glucosamine-6-phosphate
-
aminosugars
- udp-n-acetylglucosamine
- udp-glcnac
-
dynlrb1
-
n-acetylneuraminic
- dynein
-
roadblock
- mannac
-
2-epimerase
- analysis
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-acetylamino-2-deoxy-D-glucose kinase
-
-
-
-
acetylaminodeoxyglucokinase
-
-
-
-
acetylglucosamine kinase(phosphorylating)
-
-
-
-
ATP:2-acetylamino-2-deoxy-D-glucose 6-phosphotransferase
-
-
-
-
N-acetyl-D-glucosamine kinase
NagK
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:N-acetyl-D-glucosamine 6-phosphotransferase
The bacterial enzyme also acts on D-glucose.
CAS REGISTRY NUMBER
COMMENTARY
9027-48-9
-
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-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
-
roughly 50% of activity
-
-
?
N-acetylglucosamine + ATP
N-acetylglucosamine 6-phosphate + ADP
-
predominantely beta-N-acetylglucosamine 6-phosphate
-
?
additional information
?
-
-
D-fructose, D-galactose, galactosamine, N-acetyl-D-galactosamine, mannosamine, N-acetyl-D-mannosamine do not serve as substrates
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
-
part of glycoprotein synthesis pathway
-
?
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-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
-
part of glycoprotein synthesis pathway
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
the enzyme promotes the axonal growth of developing neurons
physiological function
enzyme-dynein interaction with the involvements of Lis1 and NudE1 plays an important role in prophase nuclear envelope breakdown and metaphase MT-KT attachment during eukaryotic cell division
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). NAGK_HUMAN
344
0
37376
Swiss-Prot
other Location (Reliability: 2)
C9JEV6_HUMAN
293
0
32018
TrEMBL
other Location (Reliability: 5)
H7C3G9_HUMAN
340
0
36888
TrEMBL
other Location (Reliability: 2)
H0YC94_HUMAN
136
0
14627
TrEMBL
other Location (Reliability: 1)
H0YEB7_HUMAN
182
0
19505
TrEMBL
other Location (Reliability: 2)
H7C1L7_HUMAN
159
0
16516
TrEMBL
other Location (Reliability: 2)
A0A384N6G7_HUMAN
344
0
37376
TrEMBL
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
unstable to dialysis and gel filtration, 0.013 mM substrate protects against inactivation
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
glutathione Sepharose column chromatography, MonoQ HR 5/5 column chromatography, and Superdex75 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
functionally expressed in Escherichia coli as glutathione-S-transferase fusion protein, active enzyme
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme is highly expressed from the beginning of morphological differentiation of hippocampal neurons
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Weidanz, J.A.; Campbell, P.; Moore, D.; deLucas, L.J.; Roden, L.; Thompson, J.N.; Vezza, P.
N-Acetylglucosamine kinase and N-acetylglucosamine 6-phosphate deacetylase in normal human erythrocytes and Plasmodium falciparum
Br. J. Haematol.
95
645-653
1996
Homo sapiens, Plasmodium falciparum
Gindzienski, A.; Glowacka, D.; Zwierz, K.
Purification and properties of N-acetylglucosamine kinase from human gastric mucosa
Eur. J. Biochem.
43
155-160
1974
Homo sapiens
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
Yamada-Okabe, T.; Sakamori, Y.; Mio, T.; Yamada-Okabe, H.
Identification and characterization of the genes for N-acetylglucosamine kinase and N-acetylglucosamine-phosphate deacetylase in the pathogenic fungus Candida albicans
Eur. J. Biochem.
268
2498-2505
2001
Candida albicans, Homo sapiens
Weihofen, W.A.; Berger, M.; Chen, H.; Saenger, W.; Hinderlich, S.
Structures of human N-acetylglucosamine kinase in two complexes with N-acetylglucosamine and with ADP/glucose: insights into substrate specificity and regulation
J. Mol. Biol.
364
388-399
2006
Homo sapiens (Q9UJ70), Homo sapiens
Blume, A.; Berger, M.; Benie, A.J.; Peters, T.; Hinderlich, S.
Characterization of ligand binding to N-acetylglucosamine kinase studied by STD NMR
Biochemistry
47
13138-13146
2008
Homo sapiens (Q9UJ70), Homo sapiens
Islam, M.A.; Sharif, S.R.; Lee, H.; Moon, I.S.
N-acetyl-D-glucosamine kinase promotes the axonal growth of developing neurons
Mol. Cells
38
876-885
2015
Homo sapiens
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