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Journal of Lipid Research, Vol. 9, 525-531, July 1968
Copyright © 1968 by Lipid Research, Inc.

Specificity of acyl-CoA:phospholipid acyltransferases: solvent and temperature effects

Peter Jezyk and William E. M. Lands

Department of Biological Chemistry, The University of Michigan, Ann Arbor, Michigan 48104

Acyltransfer from CoA thiol esters to either the 1- or 2-position of monoacylglycerophosphoryl choline, which is catalyzed by a microsomal preparation from rat liver, had a temperature optimum of 30-35°C. No significant alteration was observed in the ability of the acyltransferases to distinguish among the various thiol esters tested in the range of 15-40°C.

Acyl-CoA:1-acylglycerophosphoryl choline acyltransferase activity is inhibited by urea, N-alkyl ureas, and short-chain alcohols. The effect is not equal for all acyl derivatives, and ethylene glycol has much less inhibitory effect on the transfer of acids with an n — 6 (ohgr6) double bond. On the other hand, this inhibition of acyltransfer was relatively insensitive to the configuration of the Dgr9-double bond of octadecadienoates.

The specificity of the enzyme-catalyzed transfer of different acids to the 2-position can be correlated in part with the dissociation constants for the urea clathrate complexes.

Added glycol does not appreciably alter the specificity of enzyme-catalyzed transfer to the 1-position, but it inhibits the transfer of all acids in a similar fashion.

Supplementary key words acyl-CoA:monoacylglycerophosphoryl choline acyltransferase • acyltransferase selectivity • 1- and 2-acylglycerophosphenyl cholines • solvent effects • temperature optimum • essential fatty acids • urea complexes

Submitted on February 19, 1968
Accepted on March 21, 1968


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 Proc. Natl. Acad. Sci. USAHome page
E. Soupene, H. Fyrst, and F. A. Kuypers
Mammalian acyl-CoA:lysophosphatidylcholine acyltransferase enzymes
PNAS, January 8, 2008; 105(1): 88 - 93.
[Abstract] [Full Text] [PDF]


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