Issue 87, 2016
From the journal:

Chemical Communications

Substrate scope for trimethyllysine hydroxylase catalysis†

Abbas H. K. Al Temimi,‡a   Bas J. G. E. Pieters,‡a   Y. Vijayendar Reddy,a   Paul B. Whitea  and  Jasmin Mecinović*a  

* Corresponding authors

a Institute for Molecules and Materials, Radboud University, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands
E-mail: j.mecinovic@science.ru.nl
Fax: +31 (0)24 3653391
Tel: +31 (0)24 3652381

Abstract

Trimethyllysine hydroxylase (TMLH) is a non-haem Fe(II) and 2-oxoglutarate dependent oxygenase that catalyses the C-3 hydroxylation of an unactivated C–H bond in L-trimethyllysine in the first step of carnitine biosynthesis. The examination of trimethyllysine analogues as substrates for human TMLH reveals that the enzyme does hydroxylate substrates other than natural L-trimethyllysine.

Graphical abstract: Substrate scope for trimethyllysine hydroxylase catalysis

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Article information

DOI
https://doi.org/10.1039/C6CC07845A
Article type
Communication
Submitted
27 Sep 2016
Accepted
05 Oct 2016
First published
05 Oct 2016
This article is Open Access
Creative Commons BY license

Chem. Commun., 2016,52, 12849-12852

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Substrate scope for trimethyllysine hydroxylase catalysis

A. H. K. Al Temimi, B. J. G. E. Pieters, Y. V. Reddy, P. B. White and J. Mecinović, Chem. Commun., 2016, 52, 12849 DOI: 10.1039/C6CC07845A

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