Disease relevance of C00313

• We present here the cloning of the oxalyl-CoA decarboxylase gene from the bacterium Oxalobacter formigenes and its subsequent expression in a foreign environment [1].
• Cloning and expression of the oxalyl-CoA decarboxylase gene from the bacterium, Oxalobacter formigenes: prospects for gene therapy to control Ca-oxalate kidney stone formation [1].

High impact information on C00313

• This difference between the two enzymes may have physiological importance since oxalyl-CoA decarboxylation is an essential step in ATP generation in O. formigenes, and the decarboxylase activity is stimulated by exogenous ADP [2].
• Despite the significant degree of structural conservation between the two homologous enzymes and the similarity in catalytic mechanism to other thiamin diphosphate-dependent enzymes, the active site residues of oxalyl-CoA decarboxylase are unique [2].
• BACKGROUND AND PURPOSE: Oxalobacter formigenes is an anaerobic commensal colonic bacterium capable of degrading oxalate through the enzyme oxalyl-CoA decarboxylase [3].
• The stereochemistry of the overall pathway, cofactor requirements and substrate specificity of the hydroxylase and the cleavage enzyme, which is homologous with bacterial oxalyl-CoA decarboxylases, will be discussed [4].
• The sequence of two clones with lower mRNA abundance in ExHC rats than in SD rats was homologous to that of fatty acid synthase and oxalyl-CoA decarboxylase [5].

Associations of C00313 with other chemical compounds

• The enzyme catalyzed the thiamine PPi-dependent decarboxylation of oxalyl-CoA to formate and carbon dioxide [6].

Analytical, diagnostic and therapeutic context of C00313

• Oxalyl-coenzyme A (oxalyl-CoA) decarboxylase was purified from Oxalobacter formigenes by high-pressure liquid chromatography with hydrophobic interaction chromatography, DEAE anion-exchange chromatography, and gel permeation chromatography [6].

References