Overview for MACiE Entry M0231
EC Number: 184.108.40.206 (A member of the Lyases, Carbon-carbon lyases, Carboxy-lyases)
Enzyme Name: oxalate decarboxylase
Biological Species: Bacillus subtilis (Bacteria)
Catalytic Chain UniprotKB Accession Codes:
- O34714 - Oxalate decarboxylase oxdC
Representative PDB Code: 1uw8 - CRYSTAL STRUCTURE OF OXALATE DECARBOXYLASE (Resolution = 2.0 Å).
Display structure information
This reaction is irreversible.
Overall Comment: Oxalate decarboxylase contains two manganese centres. It is generally thought that site I (Mn1383) is catalytic and that site II (Mn1384) is structural. Further, this enzyme contains an unusual cofactor in the form of molecular oxygen, which is thought to act as an activator to the Mn(II) centre by increasing its redox potential.
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Stepwise Description of the Reaction
|Step 1||Oxalate coordinates to the Mn(II) centre.|
|Step 2||Dioxygen forms a bond to the Mn(II) centre through coligation.|
|Step 3||Glu162 activates the Mn(III)-bound oxalate through deprotonation. This causes the oxalate bridging oxygen to transfer an electron to the Mn(III) centre.|
|Step 4||The oxalate radical anion decarboxylates.|
|Step 5||The Mn(II) centre transfers an electron to the formyl intermediate carbon. The newly formed carbanion then deprotonates Glu162.|
|Step 6||Oxygen dissociates from the Mn(III) centre, regenerating the Mn(II) centre. Formate also dissociates, the exact order of dissociation is unclear.|
|Step 7||An acid, assumed to be water, protonates formate.|
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Catalytic Residues Involved
||Location of Function
Organic Cofactors for M0231
Metal Cofactors for M0231
- V. J. Just et al. (2004), J. Biol. Chem., 279, 19867-19874. A closed conformation of Bacillus subtilis oxalate decarboxylase OxdC provides evidence for the true identity of the active site.
- A. Angerhofer et al. (2007), J. Phys. Chem. B, 111, 5043-5046. Multifrequency EPR studies on the Mn(II) centers of oxalate decarboxylase.
- M. M. Whittaker et al. (2002), J. Biol. Inorg. Chem., 7, 136-145. Characterization of recombinant barley oxalate oxidase expressed by Pichia pastoris.
- D. Svedruzic et al. (2007), Arch. Biochem. Biophys., 464, 36-47. Investigating the roles of putative active site residues in the oxalate decarboxylase from Bacillus subtilis.
- M. Muthusamy et al. (2006), Biochemistry, 45, 10667-10673. Real-time monitoring of the oxalate decarboxylase reaction and probing hydron exchange in the product, formate, using fourier transform infrared spectroscopy.
- V. J. Just et al. (2007), Biochem. J., 407, 397-406. The identity of the active site of oxalate decarboxylase and the importance of the stability of active-site lid conformations.
Homologue information for M0231 (1uw8)
MACiE Homologues (within the PDB)
MACiE Homologues (within UniprotKB/SwissProt)
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