UXS1 tetramer decarboxylates UDP-glucuronate to UDP-xylose
UDP-GlcA + H+ → UDP-Xyl + CO2
- Reactome
- R-HSA-8863761
- Compartment
- Golgi lumen · Golgi membrane
- Rhea
- RHEA:23917
Inputs
- UDP-GlcACHEBI:58052, C15H19N2O18P2, Golgi lumen
- H+CHEBI:15378, H, Golgi lumen
Outputs
- UDP-XylCHEBI:57632, C14H20N2O16P2, Golgi lumen
- CO2CHEBI:16526, CO2, Golgi lumen
Catalysed by
- UDP-glucuronate decarboxylase activity of UXS1 tetramer [Golgi membrane]EC 4.1.1.35
Literature
- Structure and mechanism of human UDP-xylose synthase: evidence for a promoting role of sugar ring distortion in a three-step catalytic conversion of UDP-glucuronic acid J Biol Chem, 2012
- UDP-glucuronate decarboxylase, a key enzyme in proteoglycan synthesis: cloning, characterization, and localization J. Biol. Chem., 2002
- Human UDP-α-d-xylose synthase forms a catalytically important tetramer that has not been observed in crystal structures Biochemistry, 2013
- Man o' war mutation in UDP-α-D-xylose synthase favors the abortive catalytic cycle and uncovers a latent potential for hexamer formation Biochemistry, 2015