Isolation and characterization of carnitine acetyltransferase from S. cerevisiae

G. Kispál, Jozsef Cseko, Istvan Alkonyi, Sandor Attila

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29 Citations (Scopus)

Abstract

Carnitine acetyltransferase was isolated from yeast Saccharomyces cerevisiae with an apparent molecular weight of 400 000. The enzyme contains identical subunits of 65 000 Da. The Km values of the isolated enzyme for acetyl-CoA and for carnitine were 17.7 μM and 180 μM, respectively. Carnitine acetyltransferase is an inducible enzyme, a 15-fold increase in the enzyme activity was found when the cells were grown on glycerol instead of glucose. Carnitine acetyltransferase, similarly to citrate synthase, has a double localization (approx. 80% of the enzyme is mitochondrial), while acetyl-CoA synthetase was found only in the cytosol. In the mitochondria carnitine acetyltransferase is located in the matrix space. The incorporation of 14C into CO2 and in lipids showed a similar ratio, 2.9 and 2.6 when the substrate was [1-14C]acetate and [1-14C]acetylcarnitine, respectively. Based on these results carnitine acetyltransferase can be considered as an enzyme necessary for acetate metabolism by transporting the activated acetyl group from the cytosol into the mitochondrial matrix.

Original languageEnglish
Pages (from-to)217-222
Number of pages6
JournalBiochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism
Volume1085
Issue number2
DOIs
Publication statusPublished - Sep 11 1991

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Carnitine O-Acetyltransferase
Saccharomyces cerevisiae
Enzymes
Acetylcarnitine
Yeast
Acetates
Cytosol
Acetate-CoA Ligase
Citrate (si)-Synthase
Acetyl Coenzyme A
Mitochondria
Carnitine
Enzyme activity
Metabolism
Glycerol
Molecular weight
Lipids
Glucose
Yeasts
Molecular Weight

Keywords

  • (S. cerevisiae)
  • Enzyme characterization
  • sarnitine acetyltransferase

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Endocrinology

Cite this

Isolation and characterization of carnitine acetyltransferase from S. cerevisiae. / Kispál, G.; Cseko, Jozsef; Alkonyi, Istvan; Attila, Sandor.

In: Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism, Vol. 1085, No. 2, 11.09.1991, p. 217-222.

Research output: Contribution to journalArticle

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N2 - Carnitine acetyltransferase was isolated from yeast Saccharomyces cerevisiae with an apparent molecular weight of 400 000. The enzyme contains identical subunits of 65 000 Da. The Km values of the isolated enzyme for acetyl-CoA and for carnitine were 17.7 μM and 180 μM, respectively. Carnitine acetyltransferase is an inducible enzyme, a 15-fold increase in the enzyme activity was found when the cells were grown on glycerol instead of glucose. Carnitine acetyltransferase, similarly to citrate synthase, has a double localization (approx. 80% of the enzyme is mitochondrial), while acetyl-CoA synthetase was found only in the cytosol. In the mitochondria carnitine acetyltransferase is located in the matrix space. The incorporation of 14C into CO2 and in lipids showed a similar ratio, 2.9 and 2.6 when the substrate was [1-14C]acetate and [1-14C]acetylcarnitine, respectively. Based on these results carnitine acetyltransferase can be considered as an enzyme necessary for acetate metabolism by transporting the activated acetyl group from the cytosol into the mitochondrial matrix.

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