The Enzyme Database

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EC 1.14.11.8     
Accepted name: trimethyllysine dioxygenase
Reaction: N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2 = (3S)-3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
Other name(s): trimethyllysine α-ketoglutarate dioxygenase; TML-α-ketoglutarate dioxygenase; TML hydroxylase; 6-N,6-N,6-N-trimethyl-L-lysine,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
Systematic name: N6,N6,N6-trimethyl-L-lysine,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
Comments: Requires Fe2+ and ascorbate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 74622-49-4
References:
1.  Hulse, J.D., Ellis, S.R. and Henderson, L.M. Carnitine biosynthesis. β-Hydroxylation of trimethyllysine by an α-ketoglutarate-dependent mitochondrial dioxygenase. J. Biol. Chem. 253 (1978) 1654–1659. [PMID: 627563]
2.  Al Temimi, A.H., Pieters, B.J., Reddy, Y.V., White, P.B. and Mecinovic, J. Substrate scope for trimethyllysine hydroxylase catalysis. Chem. Commun. (Camb.) 52 (2016) 12849–12852. [PMID: 27730239]
3.  Lesniak, R.K., Markolovic, S., Tars, K. and Schofield, C.J. Human carnitine biosynthesis proceeds via (2S,3S)-3-hydroxy-Nε-trimethyllysine. Chem. Commun. (Camb.) 53 (2016) 440–442. [PMID: 27965989]
4.  Reddy, Y.V., Al Temimi, A.H., White, P.B. and Mecinovic, J. Evidence that trimethyllysine hydroxylase catalyzes the formation of (2S,3S)-3-hydroxy-Nε-trimethyllysine. Org. Lett. 19 (2017) 400–403. [PMID: 28045275]
[EC 1.14.11.8 created 1983]
 
 


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