UDP-glucuronate decarboxylase

In enzymology, an UDP-glucuronate decarboxylase (EC 4.1.1.35) is an enzyme that catalyzes the chemical reaction

UDP-D-glucuronate UDP-D-xylose + CO2
UDP-glucuronate decarboxylase
UDP-glucuronate decarboxylase 1, dimer, Human
Identifiers
EC number4.1.1.35
CAS number9024-68-4
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

Hence, this enzyme has one substrate, UDP-D-glucuronate, and two products, UDP-D-xylose and CO2.

This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is UDP-D-glucuronate carboxy-lyase (UDP-D-xylose-forming). Other names in common use include uridine-diphosphoglucuronate decarboxylase, and UDP-D-glucuronate carboxy-lyase. This enzyme participates in starch and sucrose metabolism and nucleotide sugars metabolism. It employs one cofactor, NAD+.

Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2B69 and 2BLL.

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References

    • Ankel H, Feingold DS (1965). "Biosynthesis of uridine diphosphate D-xylose. 1. Uridine diphosphate glucuronate carboxy-lyase of wheat germ". Biochemistry. 4 (11): 2468–2475. doi:10.1021/bi00887a028.


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