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PMID: 6772170 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Carnitine biosynthesis. Hydroxylation of N6-trimethyl-lysine to 3-hydroxy-N6-trimethyl-lysine.

The Biochemical journal ·Vol. 188 ·No. 2 ·1980-05-15 ·Pages 529-34

Sachan DS, Hoppel CL

Abstract

Rat kidney homogenates metabolize N6-trimethyl-lysine to N-trimethylammoniobutyrate, but not to carnitine. The first step in this conversion is the hydroxylation of trimethyl-lysine to form 3-hydroxy-N6-trimethyl-lysine. An assay system was developed in which hydroxylation of trimethyl-lysine is linear with respect to both time and homogenate protein concentration. The rate is 5 nmol of 3-hydroxy-N6-trimethyl-lysine formed/min per mg of homogenate protein. The cofactors required are ascorbate, alpha-oxoglutarate, FeSO4, and O2. Catalase and dithiothreitol give a 20% stimulation. Ca2+ produces a 2-fold increase in specific activity and cannot be replaced by Mg2+, Mn2+ or Zn2+. These last three bivalent cations lead to a decreased activity. Subcellular distribution studies demonstrate that trimethyl-lysine hydroxylase activity parallels the distribution profile of succinate dehydrogenase and citrate synthase. Thus trimethyl-lysine hydroxylase has a mitochondrial localization. Distribution of trimethyl-lysine hydroxylase activity between cortex and medulla of kidney if 67 and 33% respectively, similar to mitochondrial distribution.

MeSH Terms
Animals Calcium/pharmacology Carnitine/biosynthesis Cations, Divalent/pharmacology Edetic Acid/pharmacology Hydroxylation In Vitro Techniques Kidney/drug effects,metabolism Kinetics Lysine/analogs & derivatives,metabolism Male Mixed Function Oxygenases/metabolism Proteins/pharmacology Rats Subcellular Fractions/metabolism
Chemicals
Cations, Divalent Proteins trimethyllysine Edetic Acid Mixed Function Oxygenases trimethyl-lysine hydroxylase Lysine Carnitine Calcium
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Sachan D S
Hoppel C L
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31 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj1880529
Published
1980-05-15
Pages
529-34
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1161897
Subset
IM
External Links
PubMed source DOI: 10.1042/bj1880529 PMC Full Text View journal details
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