Tissue distribution of carnitine biosynthetic enzymes in man

Charles J. Rebouche, Andrew G. Engel

Research output: Contribution to journalArticlepeer-review

178 Scopus citations


The distribution in human tissues of enzymes which convert ε{lunate}-N-trimethyl-L-lysine to L-carnitine was studied. Existing methodology was modified and new procedures were developed to measure enzyme activities. ε{lunate}-N-Trimethyl-L-lysine was converted to γ-butyrobetaine in three enzymatic steps (hydroxylation at carbon 3, aldol cleavage between carbons 2 and 3 to yield glycine and γ-trimethlaminobutyraldehyde, and subsequent oxidation of the aldehyde) in all tissues studied (liver, brain, kidney, heart and skeletal muscle), but γ-butyrobetaine was hydroxylated to form L-carnitine only in liver, kidney and brain. γ-Butyrobetaine hydroxylase (4-trimethylaminobutyrate, 2-oxoglutarate : oxygen oxidoreductase (3-hydroxylating), EC activity in liver was dependent on the age of the subject. The activity rose from 12% in infants to 100% of the adult mean by age 15 years. No age dependence could be demonstrated for the other three enzymes studied.

Original languageEnglish (US)
Pages (from-to)22-29
Number of pages8
JournalBBA - General Subjects
Issue number1
StatePublished - Jun 5 1980


  • Carnitine biosynthesis
  • Enzyme distribution
  • Trimethyllysine
  • γ-Butyrobetaine (Man)

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology


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