Active-site probes of carnitine acyltransferases. Inhibition of carnitine acetyltransferase by hemiacetylcarnitinium, a reaction intermediate analogue

Richard D. Gandour, William J. Colucci, Terry C. Stelly, Paul S. Brady, Linda J. Brady

Research output: Contribution to journalArticle

13 Scopus citations

Abstract

Hemiacetylcarnitinium ((2S,6R:2R,6S)-6-carboxymethyl-2-hydroxy-2,4,4-trimethylmorpholinium) chloride is a relatively potent competitive inhibitor (Ki = 0.89 mM) of pigeon breast carnitine acetyltransferase (CAT) and of the crude rat liver CAT (Ki = 4.72 mM) but is neither an inhibitor nor an effective substrate for purified rat liver carnitine palmitoyltransferase (CPT). It does not inhibit state 3 oxygen consumption in isolated hepatic mitochondria using palmitioyl-CoA or palmitoylcarnitine as substrates. This compound is a reaction intermediate analogue of the proposed tetrahedral intermediate for acetyl transfer between acetylcarnitine and CoASH. Because the hemiketal carbon is chiral, a suggestion is made that one of the enantiomers has the same relative configuration as the proposed tetrahedral intermediate.

Original languageEnglish (US)
Pages (from-to)735-741
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume138
Issue number2
DOIs
StatePublished - Jul 31 1986

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