Thiolases of Escherichia coli: purification and chain length specificities.
The presence of only one thiolase (EC 2.3.1.9) in wild-type Escherichia coli induced for enzymes of beta oxidation was demonstrated. A different thiolase was shown to be present in a mutant constitutive for the enzymes of butyrate degradation. The two thiolases were purified to near homogeneity by a simple two-step procedure and were found to be associated with different proteins as shown by gel electrophoresis. The thiolase isolated from induced wild-type Escherichia coli cell was active on beta-ketoacyl-coenzyme A derivatives containing 4 to 16 carbons, but exhibited optimal activity with medium-chain substrates. In contrast, the thiolase isolated from the constitutive mutant was shown to be specific for acetoacetyl-coenzyme A.
D000101:Acetyl-CoA C-Acetyltransferase / Q000302:isolation & purification / Q000378:metabolism; D000123:Acetyltransferases; D002087:Butyrates; D002458:Cell Fractionation; D002845:Chromatography; D003065:Coenzyme A / Q000032:analysis / Q000378:metabolism; D004589:Electrophoresis, Disc; D004926:Escherichia coli / Q000201:enzymology*; D005227:Fatty Acids / Q000378:metabolism; D006358:Hot Temperature; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism; D010084:Oxidation-Reduction
D002087:Butyrates; D005227:Fatty Acids; D007527:Isoenzymes; D000123:Acetyltransferases; D000101:Acetyl-CoA C-Acetyltransferase; D003065:Coenzyme A