Abstract
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 1.14.11.1) 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 language | English (US) |
|---|---|
| Pages (from-to) | 22-29 |
| Number of pages | 8 |
| Journal | BBA - General Subjects |
| Volume | 630 |
| Issue number | 1 |
| DOIs | |
| State | Published - Jun 5 1980 |
Keywords
- Carnitine biosynthesis
- Enzyme distribution
- Trimethyllysine
- γ-Butyrobetaine (Man)
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
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