Decarboxylation of malonyl-CoA by lactating bovine mammary fatty acid synthase.
1. A pronounced malonyl-CoA decarboxylase activity of bovine mammary fatty acid synthase results in the formation of acetyl-CoA and not of triacetic acid lactone as in the reaction by yeast and pigeon liver synthase. 2. This activity is unaffected by the dissociation of the enzyme and is insensitive to its modification by iodoacetamide, N-ethylmaleimide, p-hydroxymercuribenzoate or 2-chloroacetyl-CoA. 3. A 50% inhibition of the activity observed on the depletion of free CoA from the medium indicates that at least part of the reaction occurs only after the acylation of the enzyme with the malonyl group. 4. A parallel reaction without such a transfer also appears to occur simultaneously.
Svoronos
S
S
Department of Chemistry, Georgetown University, Washington, DC 20057.
Kumar
S
S
D000214:Acyl Coenzyme A / Q000378:metabolism*; D000273:Adipose Tissue / Q000201:enzymology; D000818:Animals; D002417:Cattle; D003653:Decarboxylation; D064429:Fatty Acid Synthases / Q000378:metabolism*; D005260:Female; D007700:Kinetics; D007774:Lactation; D008099:Liver / Q000201:enzymology; D008316:Malonyl Coenzyme A / Q000378:metabolism*; D008321:Mammary Glands, Animal / Q000201:enzymology*; D009928:Organ Specificity; D011247:Pregnancy; D013045:Species Specificity
D000214:Acyl Coenzyme A; D008316:Malonyl Coenzyme A; D064429:Fatty Acid Synthases