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Information on EC 2.7.1.59 - N-acetylglucosamine kinase and Organism(s) Candida albicans and UniProt Accession Q59RW5
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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: Candida albicans
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)
-
-
-
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ATP:2-acetylamino-2-deoxy-D-glucose 6-phosphotransferase
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-
-
-
CaNag5p
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-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
Q59RG5
-
-
-
?
CTP + N-acetyl-D-glucosamine
CDP + N-acetyl-D-glucosamine 6-phosphate
-
-
-
-
?
dATP + N-acetyl-D-glucosamine
dADP + 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
-
highly specific
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
-
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
-
first reaction of inducible N-acetylglucosamine catabolic pathway, enables organism to grow on N-acetylglucosamine as sole carbon source
-
?
additional information
?
-
-
D-fructose, D-galactose, galactosamine, N-acetyl-D-galactosamine, mannosamine, N-acetyl-D-mannosamine do not serve as substrates
-
-
?
additional information
?
-
-
interaction of HXK1 with histone deacetylase SIR2 under filamentation inducing conditions
-
-
?
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
Q59RG5
-
-
-
?
additional information
?
-
-
interaction of HXK1 with histone deacetylase SIR2 under filamentation inducing conditions
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
-
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
-
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
-
first reaction of inducible N-acetylglucosamine catabolic pathway, enables organism to grow on N-acetylglucosamine as sole carbon source
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
physiological function
-
the enzyme regulates white-gray-opaque transitions in Candida albicans
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0-2°C, 20 mM potassium phosphate, pH 7.6, 1 mM EDTA, 10 mM 2-mercaptoethanol, stable for at least 1 week
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinnat TAP- and His-tagged HXK1 by tandem affinity purification using anti-FLAG and Ni-nitrilotriacetic acid agarose
-
CLONED (Commentary)
ORGANISM
UNIPROT
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
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rai, Y.P.; Singh, B.; Elango, N.; Datta, A.
Purification and some properties of inducible N-acetylglucosamine kinase from Candida albicans
Biochim. Biophys. Acta
614
350-356
1980
Candida albicans
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
Scarcelli, J.J.; Colussi, P.A.; Fabre, A.L.; Boles, E.; Orlean, P.; Taron, C.H.
Uptake of radiolabeled GlcNAc into Saccharomyces cerevisiae via native hexose transporters and its in vivo incorporation into GPI precursors in cells expressing heterologous GlcNAc kinase
FEMS Yeast Res.
12
305-316
2012
no activity in Saccharomyces cerevisiae, Candida albicans (Q59RG5)
Rao, K.H.; Ghosh, S.; Natarajan, K.; Datta, A.
N-acetylglucosamine kinase, HXK1 is involved in morphogenetic transition and metabolic gene expression in Candida albicans
PLoS ONE
8
e53638
2013
Candida albicans
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