A closed conformation of Bacillus subtilis oxalate decarboxylase OxdC provides evidence for the true identity of the active site.
D001412:Bacillus subtilis / Q000201:enzymology*; D001665:Binding Sites; D002245:Carbon Dioxide / Q000737:chemistry; D002262:Carboxy-Lyases / Q000737:chemistry*; D002384:Catalysis; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D005609:Free Radicals; D018698:Glutamic Acid / Q000737:chemistry; D006861:Hydrogen Peroxide / Q000737:chemistry; D007700:Kinetics; D008345:Manganese / Q000737:chemistry; D008956:Models, Chemical; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D009154:Mutation; D010088:Oxidoreductases / Q000737:chemistry; D010100:Oxygen / Q000737:chemistry; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D011522:Protons; D012997:Solvents / Q000494:pharmacology
D005609:Free Radicals; D011522:Protons; D012997:Solvents; D002245:Carbon Dioxide; D018698:Glutamic Acid; D008345:Manganese; D006861:Hydrogen Peroxide; D010088:Oxidoreductases; C020598:oxalate oxidase; D002262:Carboxy-Lyases; C021915:oxalate decarboxylase; D010100:Oxygen