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 | ||||||||
| |||||||||
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 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
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.