Trimethyllysine dioxygenase

trimethyllysine dioxygenase
Identifiers
EC number	1.14.11.8
CAS number	74622-49-4
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / EGO
Search PMC articles PubMed articles NCBI proteins

In enzymology, a trimethyllysine dioxygenase (EC 1.14.11.8) is an enzyme that catalyzes the chemical reaction

N₆,N₆,N₆-trimethyl-L-lysine + 2-oxoglutarate + O₂ $\rightleftharpoons$ 3-hydroxy-N₆,N₆,N₆-trimethyl-L-lysine + succinate + CO₂

The 3 substrates of this enzyme are N6,N6,N6-trimethyl-L-lysine, 2-oxoglutarate, and O₂, whereas its 3 products are 3-hydroxy-N6,N6,N6-trimethyl-L-lysine, succinate, and CO₂.

This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with 2-oxoglutarate as one donor, and incorporation of one atom o oxygen into each donor. The systematic name of this enzyme class is N6,N6,N6-trimethyl-L-lysine,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating). Other names in common use include trimethyllysine alpha-ketoglutarate dioxygenase, TML-alpha-ketoglutarate dioxygenase, TML hydroxylase, 6-N,6-N,6-N-trimethyl-L-lysine,2-oxoglutarate:oxygen oxidoreductase, and (3-hydroxylating). This enzyme participates in lysine degradation and L-carnitine biosynthesis. It has 3 cofactors: iron, Ascorbate, and Fe²⁺.

See also

• Carnitine biosynthesis
• γ-Butyrobetaine hydroxylase
• 4-N-Trimethylaminobutyraldehyde dehydrogenase

References

• Hulse JD, Ellis SR, Henderson LM (1978). "Carnitine biosynthesis. beta-Hydroxylation of trimethyllysine by an alpha-ketoglutarate-dependent mitochondrial dioxygenase". J. Biol. Chem. 253 (5): 1654–9. PMID 627563.
• Pastore, Annalisa; Servillo, Luigi; Giovane, Alfonso; Cautela, Domenico; Castaldo, Domenico; Balestrieri, Maria Luisa (2014). "Where Does Nε-Trimethyllysine for the Carnitine Biosynthesis in Mammals Come from?". PLoS ONE 9 (1): e84589. doi:10.1371/journal.pone.0084589. ISSN 1932-6203.