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Article

Functional analysis of TMLH variants and definition of domains required for catalytic activity and mitochondrial targeting.

Journal of cellular physiology - 1 Sept 2005

Monfregola Jlenia, Cevenini Armando, Terracciano Antonio, van Vlies Naomi, Arbucci Salvatore, Wanders Ronald J A, D'Urso Michele, Vaz Frédéric M, Ursini Matilde Valeria

Abstract excerpt

epsilon-N-Trimethyllysine hydroxylase (TMLH) (EC 1.14.11.8) is a non-heme-ferrous iron hydroxylase, Fe(++) and 2-oxoglutarate (2OG) dependent, catalyzing the first of four enzymatic reactions of the highly conserved carnitine biosynthetic pathway. Otherwise from all the other enzymes of carnitine biosynthesis, TMLH was found to be associated to the mitochondrial fraction. We here report molecular cloning of two...

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PMID: 15754339
DOI: 10.1002/jcp.20332

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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