Trimethyllysine dioxygenase

From Wikipedia, the free encyclopedia
trimethyllysine dioxygenase
Identifiers
EC no.1.14.11.8
CAS no.74622-49-4
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

In enzymology, a trimethyllysine dioxygenase (TMLH; 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

TMLH is a member of the alpha-ketoglutarate-dependent hydroxylases superfamily. The 3 substrates of this enzyme are , 2-oxoglutarate, and O2, whereas its 3 products are , 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 and requires the presence of iron and ascorbate.

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. doi:10.1016/S0021-9258(17)34915-3. 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. PMC 3890275. PMID 24454731.


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