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Chemical Compound Review

AC1L96VT     2-[3-[[4-[[[(2R,3S,4R,5R)-5- (6-aminopurin...

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Disease relevance of C00313


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


Analytical, diagnostic and therapeutic context of C00313


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