Carnitine biosynthesis in Neurospora crassa

Identification of a cDNA coding for ε-N-trimethyllysine hydroxylase and its functional expression in Saccharomyces cerevisiae

Jan H. Swiegers, Frédéric M. Vaz, Isak S. Pretorius, Ronald J A Wanders, Florian F. Bauer*

*Corresponding author for this work

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

The biosynthesis of L-carnitine in eukaryotic organisms was first elucidated in the ascomycete Neurospora crassa. The first step of the pathway is catalysed by ε-N-trimethyllysine hydroxylase (TMLH), which converts ε-N-trimethyllysine into β-hydroxy-N-ε-trimethyllysine in a reaction dependent on α-ketoglutarate, Fe2+ and oxygen. Here we report on the cloning of the N. crassa TMLH cDNA and its functional expression in Saccharomyces cerevisiae. The TMLH cDNA contains an open reading frame of 1413 base pairs encoding a predicted polypeptide of 471 amino acids. The Michaelis-Menten constants of the heterologously expressed enzyme were determined for ε-N-trimethyllysine, α-ketoglutarate, Fe2+ and correspond to 0.33 mM, 133 μM and 46 μM, respectively.

Original languageEnglish
Pages (from-to)19-23
Number of pages5
JournalFEMS Microbiology Letters
Volume210
Issue number1
DOIs
Publication statusPublished - 23 Apr 2002
Externally publishedYes

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