N-acetyl-D-glucosamine kinase

N-acetyl-D-glucosamine kinase
Identifiers
Aliases	N-acetyl-D-glucosamine_kinaseIPR023505
External IDs	GeneCards:
Orthologs
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	n ; a
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	Wikidata
View/Edit Human

Last updated December 15, 2023

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]

Related Research Articles

Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase is an enzyme that in humans is encoded by the GNE gene.

Serine/threonine-protein kinase PCTAIRE-1 is an enzyme that in humans is encoded by the PCTK1 gene.

Serine/threonine-protein kinase tousled-like 1 is an enzyme that in humans is encoded by the TLK1 gene.

Ubiquitin-conjugating enzyme E2 D3 is a protein that in humans is encoded by the UBE2D3 gene.

N-acylglucosamine 2-epimerase is an enzyme that in humans is encoded by the RENBP gene.

Ubiquitin specific peptidase 5 is an enzyme that in humans is encoded by the USP5 gene.

Tripartite motif-containing protein 29 is a protein that in humans is encoded by the TRIM29 gene.

MAP/microtubule affinity-regulating kinase 3 is an enzyme that in humans is encoded by the MARK3 gene.

Serine/threonine-protein kinase SRPK2 is an enzyme that in humans is encoded by the SRPK2 gene.

A kinase anchor protein 10, mitochondrial is an enzyme that in humans is encoded by the AKAP10 gene.

Serine/threonine-protein kinase 16 is an enzyme that in humans is encoded by the STK16 gene.

Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase is an enzyme that in humans is encoded by the MGAT1 gene.

MOB kinase activator 1A is an enzyme that in humans is encoded by the MOB1A gene.

Peroxisome assembly protein 26 is a protein that in humans is encoded by the PEX26 gene.

MAP/microtubule affinity-regulating kinase 4 is an enzyme that in humans is encoded by the MARK4 gene. MARK4 belongs to the family of serine/threonine kinases that phosphorylate microtubule-associated proteins (MAP) causing their detachment from microtubules. Detachment thereby increases microtubule dynamics and facilitates a number of cell activities including cell division, cell cycle control, cell polarity determination, and cell shape alterations.

Sialidase-4 is an enzyme that in humans is encoded by the NEU4 gene.

Brain-enriched guanylate kinase-associated protein is an enzyme that in humans is encoded by the BEGAIN gene.

E3 ubiquitin-protein ligase RNF25 is an enzyme that in humans is encoded by the RNF25 gene.

Protein O-GlcNAc transferase also known as OGT or O-linked N-acetylglucosaminyltransferase is an enzyme that in humans is encoded by the OGT gene. OGT catalyzes the addition of the O-GlcNAc post-translational modification to proteins.

O-GlcNAc is a reversible enzymatic post-translational modification that is found on serine and threonine residues of nucleocytoplasmic proteins. The modification is characterized by a β-glycosidic bond between the hydroxyl group of serine or threonine side chains and N-acetylglucosamine (GlcNAc). O-GlcNAc differs from other forms of protein glycosylation: (i) O-GlcNAc is not elongated or modified to form more complex glycan structures, (ii) O-GlcNAc is almost exclusively found on nuclear and cytoplasmic proteins rather than membrane proteins and secretory proteins, and (iii) O-GlcNAc is a highly dynamic modification that turns over more rapidly than the proteins which it modifies. O-GlcNAc is conserved across metazoans.

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. 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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.

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. S2CID 40747266.
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 (BBA) - General Subjects. 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. S2CID 22665513.
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. S2CID 23783563.
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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
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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[pmid10824116-1] 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. 267 (11): 3301–8. doi: 10.1046/j.1432-1327.2000.01360.x . PMID 10824116.

[entrez-2] 1 2 "Entrez Gene: NAGK N-acetylglucosamine kinase".

[pmid11741987-3] 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.

[pmid16189514-4] 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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.

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N-acetyl-D-glucosamine kinase

Contents

Function

Interactions

Related Research Articles

References

Further reading