title: Propionyl-coenzyme A carboxylase of Mycobacterium smegmatis. An electron microscopic study.
abstract: Propionyl-CoA carboxylase has been purified to homogeneity and examined in electron microscope. The native carboxylase presents a profile with a large central subunit to which smaller subunits are attached. The central subunit has two prominent profiles, one circular (100 A) with a central hole and the other rectangular (70 X 100 A). The six polypeptides of this subunit appear to be arranged in a cylindrical structure. Six spherical (50 A) biotin-containing peripheral subunits are attached in sets of three to the two opposite circular faces of the central subunit. A model of the 18-S carboxylase is presented.
mesh_terms: D002262:Carboxy-Lyases / Q000302:isolation & purification*; D055598:Chemical Phenomena; D002621:Chemistry; D043586:Methylmalonyl-CoA Decarboxylase; D008854:Microscopy, Electron; D008958:Models, Molecular; D009161:Mycobacterium / Q000201:enzymology* / Q000648:ultrastructure; D010446:Peptide Fragments; D011487:Protein Conformation
chemical_list: D010446:Peptide Fragments; D002262:Carboxy-Lyases; D043586:Methylmalonyl-CoA Decarboxylase