N-acetyl-D-glucosamine kinase

NAGK
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
Aliases NAGK, Nagk, Gnk, HSA242910, N-acetylglucosamine kinase
External IDs MGI: 1860418 HomoloGene: 9720 GeneCards: NAGK
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez

55577

56174

Ensembl

ENSG00000124357

ENSMUSG00000034744

UniProt

Q9UJ70

Q9QZ08

RefSeq (mRNA)

NM_017567

NM_001164187
NM_019542

RefSeq (protein)

NP_060037.3

NP_062415.1

Location (UCSC) Chr 2: 71.06 – 71.08 Mb Chr 6: 83.79 – 83.8 Mb
PubMed search [1] [2]
Wikidata
View/Edit HumanView/Edit Mouse

N-acetyl-D-glucosamine kinase is an enzyme that in humans is encoded by the NAGK gene.[3][4]

Function

N-acetylglucosamine kinase (NAGK; EC 2.7.1.59) converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate. NAGK belongs to the group of N-acetylhexosamine kinases and is a prominent salvage enzyme of amino sugar metabolism in mammals.[supplied by OMIM][4]

Interactions

NAGK has been shown to interact with STK16[5] and LNX1.[6]

References

  1. ↑ "Human PubMed Reference:".
  2. ↑ "Mouse PubMed Reference:".
  3. ↑ Hinderlich S, Berger M, Schwarzkopf M, Effertz K, Reutter W (Jun 2000). "Molecular cloning and characterization of murine and human N-acetylglucosamine kinase". European Journal of Biochemistry / FEBS. 267 (11): 3301–8. doi:10.1046/j.1432-1327.2000.01360.x. PMID 10824116.
  4. 1 2 "Entrez Gene: NAGK N-acetylglucosamine kinase".
  5. ↑ Ligos JM, de Lera TL, Hinderlich S, Guinea B, Sánchez L, Roca R, Valencia A, Bernad A (Feb 2002). "Functional interaction between the Ser/Thr kinase PKL12 and N-acetylglucosamine kinase, a prominent enzyme implicated in the salvage pathway for GlcNAc recycling". The Journal of Biological Chemistry. 277 (8): 6333–43. doi:10.1074/jbc.M105766200. PMID 11741987.
  6. ↑ Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.

Further reading

  • Maruyama K, Sugano S (Jan 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1-2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298. 
  • Weidanz JA, Campbell P, Moore D, DeLucas LJ, Rodén L, Thompson JN, Vezza AC (Dec 1996). "N-acetylglucosamine kinase and N-acetylglucosamine 6-phosphate deacetylase in normal human erythrocytes and Plasmodium falciparum". British Journal of Haematology. 95 (4): 645–53. doi:10.1046/j.1365-2141.1996.d01-1955.x. PMID 8982040. 
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (Oct 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1-2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149. 
  • Lowes W, Walker M, Alberti KG, Agius L (Jan 1998). "Hexokinase isoenzymes in normal and cirrhotic human liver: suppression of glucokinase in cirrhosis". Biochimica et Biophysica Acta. 1379 (1): 134–42. doi:10.1016/s0304-4165(97)00092-5. PMID 9468341. 
  • Ligos JM, de Lera TL, Hinderlich S, Guinea B, Sánchez L, Roca R, Valencia A, Bernad A (Feb 2002). "Functional interaction between the Ser/Thr kinase PKL12 and N-acetylglucosamine kinase, a prominent enzyme implicated in the salvage pathway for GlcNAc recycling". The Journal of Biological Chemistry. 277 (8): 6333–43. doi:10.1074/jbc.M105766200. PMID 11741987. 
  • Maguire PB, Wynne KJ, Harney DF, O'Donoghue NM, Stephens G, Fitzgerald DJ (Jun 2002). "Identification of the phosphotyrosine proteome from thrombin activated platelets". Proteomics. 2 (6): 642–8. doi:10.1002/1615-9861(200206)2:6<642::AID-PROT642>3.0.CO;2-I. PMID 12112843. 
  • Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J (May 2003). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nature Biotechnology. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801. 
  • Lehner B, Sanderson CM (Jul 2004). "A protein interaction framework for human mRNA degradation". Genome Research. 14 (7): 1315–23. doi:10.1101/gr.2122004. PMC 442147Freely accessible. PMID 15231747. 
  • Sparks SE, Ciccone C, Lalor M, Orvisky E, Klootwijk R, Savelkoul PJ, Dalakas MC, Krasnewich DM, Gahl WA, Huizing M (Nov 2005). "Use of a cell-free system to determine UDP-N-acetylglucosamine 2-epimerase and N-acetylmannosamine kinase activities in human hereditary inclusion body myopathy". Glycobiology. 15 (11): 1102–10. doi:10.1093/glycob/cwi100. PMID 15987957. 
  • Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514. 
  • Weihofen WA, Berger M, Chen H, Saenger W, Hinderlich S (Dec 2006). "Structures of human N-Acetylglucosamine kinase in two complexes with N-Acetylglucosamine and with ADP/glucose: insights into substrate specificity and regulation". Journal of Molecular Biology. 364 (3): 388–99. doi:10.1016/j.jmb.2006.08.085. PMID 17010375. 


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