UDP-glucuronate decarboxylase | |||||||||
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Identifiers | |||||||||
EC no. | 4.1.1.35 | ||||||||
CAS no. | 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 / QuickGO | ||||||||
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The enzyme UDP-glucuronate decarboxylase (EC 4.1.1.35) catalyzes the chemical reaction
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+.
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2B69 and 2BLL.
Carboxy-lyases, also known as decarboxylases, are carbon–carbon lyases that add or remove a carboxyl group from organic compounds. These enzymes catalyze the decarboxylation of amino acids, beta-keto acids and alpha-keto acids.
In enzymology, an UDP-arabinose 4-epimerase is an enzyme that catalyzes the chemical reaction
In enzymology, an UDP-glucuronate 4-epimerase is an enzyme that catalyzes the chemical reaction
In enzymology, an UDP-glucuronate 5'-epimerase is an enzyme that catalyzes the chemical reaction
The enzyme 2-oxoglutarate decarboxylase (EC 4.1.1.71) catalyzes the chemical reaction: 2-oxoglutarate succinate semialdehyde + CO2
The enzyme 3-dehydro-L-gulonate-6-phosphate decarboxylase (EC 4.1.1.85) catalyzes the chemical reaction
The enzyme aconitate decarboxylase (EC 4.1.1.6) catalyzes the chemical reaction
The enzyme aminocarboxymuconate-semialdehyde decarboxylase (EC 4.1.1.45) catalyzes the chemical reaction
The enzyme benzoylformate decarboxylase (EC 4.1.1.7) catalyzes the following chemical reaction:
The enzyme dehydro-L-gulonate decarboxylase (EC 4.1.1.34) catalyzes the chemical reaction
Diphosphomevalonate decarboxylase (EC 4.1.1.33), most commonly referred to in scientific literature as mevalonate diphosphate decarboxylase, is an enzyme that catalyzes the chemical reaction
The enzyme oxalyl-CoA decarboxylase (OXC) (EC 4.1.1.8), primarily produced by the gastrointestinal bacterium Oxalobacter formigenes, catalyzes the chemical reaction
The enzyme phosphatidylserine decarboxylase (EC 4.1.1.65) catalyzes the chemical reaction
The enzyme phosphonopyruvate decarboxylase (EC 4.1.1.82) catalyzes the chemical reaction
The enzyme UDP-galacturonate decarboxylase (EC 4.1.1.67) catalyzes the chemical reaction
In enzymology, a 1,4-beta-D-xylan synthase is an enzyme that catalyzes the chemical reaction
In enzymology, a glucuronate-1-phosphate uridylyltransferase is an enzyme that catalyzes the chemical reaction
In enzymology, an UTP—xylose-1-phosphate uridylyltransferase is an enzyme that catalyzes the chemical reaction
UDP-glucuronic acid decarboxylase 1 is an enzyme that in humans is encoded by the UXS1 gene.
David Sidney Feingold was an American biochemist.