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

Stable Identifier
R-HSA-6803771
Type
Reaction [transition]
Species
Homo sapiens
Compartment
Locations in the PathwayBrowser
General
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

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
21073341 Biomedical differences between human and nonhuman hominids: potential roles for uniquely human aspects of sialic acid biology

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

Annu Rev Pathol 2011
17010375 Structures of human N-Acetylglucosamine kinase in two complexes with N-Acetylglucosamine and with ADP/glucose: insights into substrate specificity and regulation

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

J. Mol. Biol. 2006
10824116 Molecular cloning and characterization of murine and human N-acetylglucosamine kinase

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

Eur. J. Biochem. 2000
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
N-acetylglucosamine kinase activity of NAGK dimer [cytosol]
Physical Entity
Activity
Orthologous Events
Authored
Reviewed
Created