title: Substrate scope for trimethyllysine hydroxylase catalysis.
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.
authors.affiliation: Institute for Molecules and Materials, Radboud University, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands. j.mecinovic@science.ru.nl.
authors.forename: Abbas H K
authors.initials: AH
authors.lastname: Al Temimi
authors.affiliation: Institute for Molecules and Materials, Radboud University, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands. j.mecinovic@science.ru.nl.
authors.forename: Bas J G E
authors.initials: BJ
authors.lastname: Pieters
authors.affiliation: Institute for Molecules and Materials, Radboud University, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands. j.mecinovic@science.ru.nl.
authors.forename: Y Vijayendar
authors.initials: YV
authors.lastname: Reddy
authors.affiliation: Institute for Molecules and Materials, Radboud University, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands. j.mecinovic@science.ru.nl.
authors.forename: Paul B
authors.initials: PB
authors.lastname: White
authors.affiliation: Institute for Molecules and Materials, Radboud University, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands. j.mecinovic@science.ru.nl.
authors.forename: Jasmin
authors.initials: J
authors.lastname: Mecinović