N-acetyl-D-glucosamine kinase
N-acetylglucosamine kinase | |||||||||||||
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PDB rendering based on 2ch5. | |||||||||||||
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Identifiers | |||||||||||||
Symbols | NAGK ; GNK; HSA242910 | ||||||||||||
External IDs | OMIM: 606828 MGI: 1860418 HomoloGene: 9720 GeneCards: NAGK Gene | ||||||||||||
EC number | 2.7.1.59 | ||||||||||||
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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 | |||||||||||
RefSeq (protein) | NP_060037 | NP_001157659 | |||||||||||
Location (UCSC) |
Chr 2: 71.06 – 71.08 Mb |
Chr 6: 83.79 – 83.8 Mb | |||||||||||
PubMed search | |||||||||||||
N-acetyl-D-glucosamine kinase is an enzyme that in humans is encoded by the NAGK gene.[1][2]
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][2]
Interactions
NAGK has been shown to interact with STK16[3] and LNX1.[4]
References
- ↑ 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.
- 1 2 "Entrez Gene: NAGK N-acetylglucosamine kinase".
- ↑ 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.
- ↑ 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 442147. 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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