GlcNAc1P is dephosphorylated to UDP-N-acetyl-glucosamine

Stable Identifier
R-HSA-446204
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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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

Peneff, C, Ferrari, P, Charrier, V, Taburet, Y, Monnier, C, Zamboni, V, Winter, J, Harnois, M, Fassy, F, Bourne, Y

EMBO J 2001
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
UDP-N-acetylglucosamine diphosphorylase activity of 2xUAP1 [cytosol]
Physical Entity
Activity
Orthologous Events
Authored
Reviewed
Created