Regulation of volatile fatty acid uptake by mitochondrial acyl CoA synthetases of bovine heart.
Purification of components of heart mitochondria activating short chain fatty acids prepared from tissue of lactating Holstein cows demonstrated predominantly one acyl CoA synthetase, acetyl CoA synthetase activating acetate, and propionate. Activity of butyryl CoA synthetase was low. Propionyl CoA synthetase characteristically in bovine liver and kidney tissue could not be demonstrated in heart mitochondria. Thus, of the ruminally derived volatile fatty acids only acetate can be used by heart mitochondria as a primary energy source because of small quantities of propionate in peripheral blood. Acetyl CoA synthetase was a glycoprotein composed of a single polypeptide chain of apparent molecular weight 67,500. The Michaelis-Menten constant for acetate was 1.8 x 10(-4)M. By comparison with literature for blood acetate concentration we concluded that enzyme is saturated with substrate at all physiological concentrations of acetate. These kinetic properties ensure a constant supply of acetate as an energy source for maintaining heart function in ruminants.
D000106:Acetate-CoA Ligase / Q000302:isolation & purification / Q000378:metabolism; D000818:Animals; D002417:Cattle / Q000378:metabolism*; D002849:Chromatography, Gas; D003066:Coenzyme A Ligases / Q000302:isolation & purification / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D005232:Fatty Acids, Volatile / Q000378:metabolism*; D008929:Mitochondria, Heart / Q000201:enzymology*; D008970:Molecular Weight
D005232:Fatty Acids, Volatile; D003066:Coenzyme A Ligases; D000106:Acetate-CoA Ligase; C019805:butyryl-CoA synthetase