title: Purification and subunit structure of propionyl coenzyme A carboxylase of Mycobacterium smegmatis.
abstract: Propionyl-CoA carboxylase (EC 6.4.1.3) has been purified from Mycobacterium smegmatis. It has a molecular weight of about 500,000. On sodium dodecyl sulfate gels it dissociates into two subunits with molecular weights of 64,000 and 57,000. There are 3.8 mol of biotin/500,000 g of protein. The biotin is associated entirely with the heavier subunit. The enzyme also used acetyl-CoA as a substrate. No other acetyl-CoA carboxylase could be detected in this organism.
mesh_terms: D000214:Acyl Coenzyme A; D000818:Animals; D001710:Biotin / Q000032:analysis; D002417:Cattle; D007668:Kidney / Q000201:enzymology; D008025:Ligases / Q000302:isolation & purification*; D046911:Macromolecular Substances; D008970:Molecular Weight; D009161:Mycobacterium / Q000201:enzymology*; D011422:Propionates; D013045:Species Specificity
chemical_list: D000214:Acyl Coenzyme A; D046911:Macromolecular Substances; D011422:Propionates; D001710:Biotin; D008025:Ligases