NAGK dimer phosphorylates GlcNAc, GlcNGc to GlcNAc-6-P, GlcNGc-6-P

Stable Identifier
Reaction [transition]
Homo sapiens
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Humans are not able to catalyse the formation of N-glycolylneuraminic acid (Neu5Gc) due to an inactive CMAHP enzyme. Neu5Gc can be obtained from dietary sources and must be degraded to avoid accummulation and resultant chronic inflammation known as xenosialitis (Varki et al. 2011). Degradation of excess Neu5Gc results in the formation of two ubiquitous metabolites involved in asparagine N-linked glycosylation; glycolate and glucosamine 6-phosphate. In the Neu5Gc degradation pathway, a salvage reaction of amino sugar metabolism utilises dimeric GlcNAc kinase (NAGK) to phosphorylate N-acetylglucosamine (GlcNAc) to GlcNAc-6-phosphate and N-glycolylglucosamine (GlcNGc) to GlcNGc-6-P (Hinderlich et al. 2000, Weihofen et al. 2006).

Literature References
PubMed ID Title Journal Year
17010375 Structures of human N-Acetylglucosamine kinase in two complexes with N-Acetylglucosamine and with ADP/glucose: insights into substrate specificity and regulation

Berger, M, Saenger, W, Weihofen, WA, Chen, H, Hinderlich, S

J. Mol. Biol. 2006
21073341 Biomedical differences between human and nonhuman hominids: potential roles for uniquely human aspects of sialic acid biology

Varki, NM, Dick, EJ, Benirschke, K, Varki, A, Strobert, E

Annu Rev Pathol 2011
10824116 Molecular cloning and characterization of murine and human N-acetylglucosamine kinase

Schwarzkopf, M, Reutter, W, Berger, M, Effertz, K, Hinderlich, S

Eur. J. Biochem. 2000
Catalyst Activity

N-acetylglucosamine kinase activity of NAGK dimer [cytosol]

Orthologous Events
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