Acetyl-CoA acetyltransferase from bovine liver mitochondria. Molecular properties of multiple forms.
Bovine liver mitochondrial acetyl-CoA acetyltransferase (acetyl-CoA:acetyl-CoA C-acetyltransferase, EC 2.3.1.9) has been obtained in three forms designated transferase I, A and B on the basis of their elution positions from chromatography on phosphocellulose. All forms have been shown to have a molecular weight of about 152 000, each being composed of four similar subunits. Amino acid analysis of transferase A and B, the two major forms, revealed a close relationship between both forms with almost identical amino acid composition and arginine as N-terminal residue. The three transferases differ with respect to their redox state and their multiplicity of forms with isoelectric points of 6.9, 7.5 and 8.8, into which the transferases I and A were spontaneously transformed upon isoelectric focusing or rechromatography on phosphocellulose. Transferase B represents a stable enzyme form with an isoelectric point of 8.8. Although the redox state of transferase B can be adjusted to that of transferase A still a difference in charge and in the multiplicity of forms exists, thus indicating different protein states.
D000101:Acetyl-CoA C-Acetyltransferase / Q000302:isolation & purification* / Q000378:metabolism; D000123:Acetyltransferases / Q000302:isolation & purification*; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D003545:Cysteine / Q000032:analysis; D004355:Drug Stability; D007526:Isoelectric Point; D046911:Macromolecular Substances; D008930:Mitochondria, Liver / Q000201:enzymology*; D008970:Molecular Weight; D010084:Oxidation-Reduction; D013438:Sulfhydryl Compounds / Q000032:analysis
D000596:Amino Acids; D046911:Macromolecular Substances; D013438:Sulfhydryl Compounds; D000123:Acetyltransferases; D000101:Acetyl-CoA C-Acetyltransferase; D003545:Cysteine