Stabilization of an acetyl-coenzyme A carboxylase complex from Pseudomonas citronellolis.
Using stabilizing conditions the acetyl-CoA carboxylase (EC 6.4.1.2) of Pseudomonas citronellolis has been isolated as a complex containing four different polypeptide chains with molecular weights of 53 000, 36 000, 33 000 and 25 000. Evidence is presented to suggest that these polypeptide chains correspond to distinct biotin carboxylase, transcarboxylase and biotin carboxyl carrier protein subunits in analogy with similar subunits of Escherichia coli acetyl-CoA carboxylase, an unstable complex in vitro.
D000103:Acetyl-CoA Carboxylase / Q000302:isolation & purification / Q000378:metabolism*; D001426:Bacterial Proteins / Q000302:isolation & purification / Q000378:metabolism; D001710:Biotin; D004926:Escherichia coli / Q000201:enzymology; D008025:Ligases / Q000302:isolation & purification / Q000378:metabolism*; D046911:Macromolecular Substances; D008764:Methylmalonic Acid; D008970:Molecular Weight; D009097:Multienzyme Complexes / Q000302:isolation & purification / Q000378:metabolism*; D011549:Pseudomonas / Q000201:enzymology*; D011773:Pyruvates; D013045:Species Specificity; D014166:Transferases / Q000302:isolation & purification / Q000378:metabolism
D001426:Bacterial Proteins; D046911:Macromolecular Substances; D009097:Multienzyme Complexes; D011773:Pyruvates; D001710:Biotin; D008764:Methylmalonic Acid; D014166:Transferases; D008025:Ligases; D000103:Acetyl-CoA Carboxylase