Biology: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 / QuickGO | ||||||||
| |||||||||
Trimethyllysine dioxygenase (TMLH; EC 1.14.11.8) is an enzyme that catalyzes the chemical reaction
- REDIRECT Template:Chemical reaction
TMLH is a member of the alpha-ketoglutarate-dependent hydroxylases superfamily. It oxidises trimethyl-L-lysine to the product (3S)-3-hydroxy-N6,N6,N6-trimethyl-L-lysine.[1][2]
This enzyme is an oxidase with the systematic name 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.[1]
Mechanism
The enzyme is a non-heme iron protein with ferryl active site where Fe(IV)=O is the species that transfers its oxygen to the substrate.[3][4]
The mechanism requires 2-oxoglutaric acid to activate the iron oxygen complex, and this gives succinic acid and carbon dioxide when the second atom of the molecular oxygen is removed. Ascorbic acid is also required to increase the turnover number of the enzyme by reducing any iron converted to Fe(III) back to the required Fe(II).[5]
- REDIRECT Template:Chemical reaction
See also
References
- ↑ 1.0 1.1 Enzyme 1.14.11.8 at KEGG Pathway Database.
- ↑ "Carnitine biosynthesis. beta-Hydroxylation of trimethyllysine by an alpha-ketoglutarate-dependent mitochondrial dioxygenase". J. Biol. Chem. 253 (5): 1654–9. 1978. 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). doi:10.1371/journal.pone.0084589. ISSN 1932-6203. PMID 24454731. Bibcode: 2014PLoSO...984589S.
- ↑ "NMR studies of the non-haem Fe(II) and 2-oxoglutarate-dependent oxygenases". J. Inorg. Biochem. 177: 384–394. December 2017. doi:10.1016/j.jinorgbio.2017.08.032. PMID 28893416.
- ↑ "Structure of proline 3-hydroxylase. Evolution of the family of 2-oxoglutarate dependent oxygenases". Eur. J. Biochem. 268 (24): 6625–36. 2001. doi:10.1046/j.0014-2956.2001.02617.x. PMID 11737217.
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