Reactome | GlcNAc1P is dephosphorylated to UDP-N-acetyl-glucosamine

GlcNAc1P is dephosphorylated to UDP-N-acetyl-glucosamine

Stable Identifier

R-HSA-446204

Type

Reaction

Species

Homo sapiens

Compartment

cytosol

Locations in the PathwayBrowser

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Metabolism of proteins (Homo sapiens)

- Post-translational protein modification (Homo sapiens)
  - Asparagine N-linked glycosylation (Homo sapiens)
    - Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein (Homo sapiens)
      - Synthesis of substrates in N-glycan biosythesis (Homo sapiens)
        
        Synthesis of UDP-N-acetyl-glucosamine (Homo sapiens)
        
        GlcNAc1P is dephosphorylated to UDP-N-acetyl-glucosamine (Homo sapiens)

General

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GlcNAc1P is dephosphorylated to UDP-N-acetyl-glucosamine

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Cytosolic UAP1 catalyzes the reaction of N-acetyl-D-glucosamine 1-phosphate (GlcNAc1P) and UTP to UDP-N-acetyl-D-glucosamine and pyrophosphate. Structural studies indicate that the active form of the enzyme is a dimer (Peneff C et al, 2001).

Literature References

PubMed ID	Title	Journal	Year
11707391	Crystal structures of two human pyrophosphorylase isoforms in complexes with UDPGlc(Gal)NAc: role of the alternatively spliced insert in the enzyme oligomeric assembly and active site architecture Fassy, F, Monnier, C, Peneff, C, Harnois, M, Ferrari, P, Bourne, Y, Charrier, V, Zamboni, V, Winter, J, Taburet, Y	EMBO J	2001