UDP-glucuronate decarboxylase

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UDP-glucuronate decarboxylase
2b69.jpg
UDP-glucuronate decarboxylase 1, dimer, Human
Identifiers
EC number 4.1.1.35
CAS number 9024-68-4
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO

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

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[edit]

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

References[edit]

  • 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.