Oxalate decarboxylase

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oxalate decarboxylase
5hi0.jpg
Oxalate decarboxylase hexamer, Bacillus subtilis
Identifiers
EC number4.1.1.2
CAS number9024-97-9
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

In enzymology, an oxalate decarboxylase (EC 4.1.1.2) is an enzyme that catalyzes the chemical reaction

oxalate + H+ formate + CO2

Thus, the two substrates of this enzyme are oxalate and H+, whereas its two products are formate 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 oxalate carboxy-lyase (formate-forming). This enzyme is also called oxalate carboxy-lyase. This enzyme participates in glyoxylate and dicarboxylate metabolism.

Structural studies[edit]

As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1UW8, 2UY8, 2UY9, 2UYA, and 2UYB.

References[edit]

  • HAYAISHI O, JAKOBY WB, OHMURA E (1956). "Enzymatic decarboxylation of oxalic acid". J. Biol. Chem. 222 (1): 435&ndash, 46. PMID 13367015.
  • Tanner A, Bornemann S (2000). "Bacillus subtilis YvrK is an acid-induced oxalate decarboxylase". J. Bacteriol. 182 (18): 5271&ndash, 3. doi:10.1128/JB.182.18.5271-5273.2000. PMC 94680. PMID 10960116.
  • Tanner A, Bowater L, Fairhurst SA, Bornemann S (2001). "Oxalate decarboxylase requires manganese and dioxygen for activity Overexpression and characterization of Bacillus subtilis YvrK and YoaN". J. Biol. Chem. 276 (47): 43627&ndash, 34. doi:10.1074/jbc.M107202200. PMID 11546787.