J. Lipid Res. Acyl Labeled PIP's available August 1, 2008
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Journal of Lipid Research, Vol 34, 95-99, Copyright © 1993 by Lipid Research, Inc.

ARTICLES

Identification of bile acid coenzyme A synthetase in rat kidney

JB Kwakye, S Barnes and RB Diasio
Department of Pharmacology, University of Alabama, Birmingham 35294.

Bile acid CoA synthetase has been discovered in rat kidney. Incubation of kidney microsomes with [14C]chenodeoxycholic acid and CoA produced a single peak with the high performance liquid chromatography (HPLC) retention time of CDC-CoA. This peak, when incubated with purified bile acid CoA: amino acid N-acyltransferase (BAT) from human liver and either taurine or glycine, led to the formation of CDC-taurine or CDC- glycine, respectively. Kinetic analysis revealed apparent Kms for CDC and CoA of 2.5 microM and 2.6 microM, respectively. This activity appeared specific for bile acids as it was not inhibited by benzoic acid or salicylic acid, known substrates for other rat kidney CoA synthetases. This demonstrates that the kidney has the potential for bile acid metabolism and may have a role in bile acid physiology.
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J. O'Byrne, M. C. Hunt, D. K. Rai, M. Saeki, and S. E. H. Alexson
The Human Bile Acid-CoA:Amino Acid N-Acyltransferase Functions in the Conjugation of Fatty Acids to Glycine
J. Biol. Chem., September 5, 2003; 278(36): 34237 - 34244.
[Abstract] [Full Text] [PDF]


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