Carnitine biosynthesis in Neurospora crassa: identification of a cDNA coding for epsilon-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

doi:https://doi.org/10.1111/j.1574-6968.2002.tb11154.x

Carnitine biosynthesis in Neurospora crassa: identification of a cDNA coding for epsilon-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

Paediatric Metabolic Diseases (AMC)

Research output: Contribution to journal › Article › Academic › peer-review

24 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 epsilon-N-trimethyllysine hydroxylase (TMLH), which converts epsilon-N-trimethyllysine into beta-hydroxy-N-epsilon-trimethyllysine in a reaction dependent on alpha-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 epsilon-N-trimethyllysine, alpha-ketoglutarate, Fe2+ and correspond to 0.33 mM, 133 microM and 46 microM, respectively

Original language	English
Pages (from-to)	19-23
Journal	FEMS Microbiology Letters
Volume	210
Issue number	1
DOIs	https://doi.org/10.1111/j.1574-6968.2002.tb11154.x
Publication status	Published - 2002

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@article{3d269a893072416b84c0a935470d0029,

title = "Carnitine biosynthesis in Neurospora crassa: identification of a cDNA coding for epsilon-N-trimethyllysine hydroxylase and its functional expression in Saccharomyces cerevisiae",

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 epsilon-N-trimethyllysine hydroxylase (TMLH), which converts epsilon-N-trimethyllysine into beta-hydroxy-N-epsilon-trimethyllysine in a reaction dependent on alpha-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 epsilon-N-trimethyllysine, alpha-ketoglutarate, Fe2+ and correspond to 0.33 mM, 133 microM and 46 microM, respectively",

author = "Swiegers, {Jan H.} and Vaz, {Fr{\'e}d{\'e}ric M.} and Pretorius, {Isak S.} and Wanders, {Ronald J. A.} and Bauer, {Florian F.}",

year = "2002",

doi = "https://doi.org/10.1111/j.1574-6968.2002.tb11154.x",

language = "English",

volume = "210",

pages = "19--23",

journal = "FEMS Microbiology Letters",

issn = "0378-1097",

publisher = "Wiley-Blackwell",

number = "1",

}

Carnitine biosynthesis in Neurospora crassa: identification of a cDNA coding for epsilon-N-trimethyllysine hydroxylase and its functional expression in Saccharomyces cerevisiae. / Swiegers, Jan H.; Vaz, Frédéric M.; Pretorius, Isak S. et al.
In: FEMS Microbiology Letters, Vol. 210, No. 1, 2002, p. 19-23.

Research output: Contribution to journal › Article › Academic › peer-review

TY - JOUR

T1 - Carnitine biosynthesis in Neurospora crassa: identification of a cDNA coding for epsilon-N-trimethyllysine hydroxylase and its functional expression in Saccharomyces cerevisiae

AU - Swiegers, Jan H.

AU - Vaz, Frédéric M.

AU - Pretorius, Isak S.

AU - Wanders, Ronald J. A.

AU - Bauer, Florian F.

PY - 2002

Y1 - 2002

N2 - 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 epsilon-N-trimethyllysine hydroxylase (TMLH), which converts epsilon-N-trimethyllysine into beta-hydroxy-N-epsilon-trimethyllysine in a reaction dependent on alpha-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 epsilon-N-trimethyllysine, alpha-ketoglutarate, Fe2+ and correspond to 0.33 mM, 133 microM and 46 microM, respectively

AB - 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 epsilon-N-trimethyllysine hydroxylase (TMLH), which converts epsilon-N-trimethyllysine into beta-hydroxy-N-epsilon-trimethyllysine in a reaction dependent on alpha-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 epsilon-N-trimethyllysine, alpha-ketoglutarate, Fe2+ and correspond to 0.33 mM, 133 microM and 46 microM, respectively

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DO - https://doi.org/10.1111/j.1574-6968.2002.tb11154.x

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SN - 0378-1097

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