Specificity of Diacylglycerol Acyltransferase from Bovine Mammary Gland, Liver and Adipose Tissue towards Acyl‐CoA Esters

Abstract

Microsomal diacylglycerol acyltransferase from bovine lactating mammary gland, liver and adipose tissue was capable of acylating microsomal‐bound 1,2‐dipalmitoylglycerol with acyl‐CoA of chain length C4–C18. The activity of the liver and adipose enzymes towards butyryl‐CoA and hexanoyl‐CoA relative to longer‐chain acyl‐CoA was similar to that of the mammary enzyme. The Km and V values of the three enzymes with butyryl‐CoA and hexanoyl‐CoA were similar, except for the V values of the adipose enzyme which were higher. Microsomal diacylglycerol acyltransferase from mammary gland and liver of non‐ruminants was also capable of utilizing butyryl‐CoA. These results indicate that the unique presence of short‐chain acids in ruminant milk triacylglycerols is not caused by differences in specificity between the diacylglycerol acyltransferase from ruminant mammary and other tissues. Copyright © 1979, Wiley Blackwell. All rights reserved