| EC Tree |
| 1. Oxidoreductases |
| 1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen |
| 1.14.11 With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor |
| ID: | 1.14.11.8 |
|---|---|
| Description: | Trimethyllysine dioxygenase. |
| Alternative Name: |
Trimethyllysine,2-oxoglutarate dioxygenase. Trimethyllysine alpha-ketoglutarate dioxygenase. TMLD. TML-alpha-ketoglutarate dioxygenase. TML hydroxylase. TML dioxygenase. Epsilon-trimethyllysine 2-oxoglutarate dioxygenase. |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.| UniProtKB Enzyme Link: | UniProtKB 1.14.11.8 |
| BRENDA Enzyme Link: | BRENDA 1.14.11.8 |
| KEGG Enzyme Link: | KEGG1.14.11.8 |
| BioCyc Enzyme Link: | BioCyc 1.14.11.8 |
| ExPASy Enzyme Link: | ExPASy1.14.11.8 |
| EC2PDB Enzyme Link: | EC2PDB 1.14.11.8 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.14.11.8 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.14.11.8 |
| IntEnz Enzyme Link: | IntEnz 1.14.11.8 |
| MEDLINE Enzyme Link: | MEDLINE 1.14.11.8 |
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:14181 | 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysine + O2 = (3S)-3-hydroxy-N(6),N(6),N(6)-trimethyl-L-lysine + CO2 + succinate |
| RULE(radius=1) | [*:1]-[CH2;+0:2]-[*:3].[*:4]=[C;H0;+0:5](-[OH;+0:6])-[C;H0;+0:7](=[*:8])-[*:9].[O;H0;+0:10]=[O;H0;+0:11]>>[*:1]-[CH;+0:2](-[*:3])-[OH;+0:10].[*:8]=[C;H0;+0:7](-[*:9])-[OH;+0:11].[*:4]=[C;H0;+0:5]=[O;H0;+0:6] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Carnitine biosynthesis. beta-Hydroxylation of trimethyllysine by an alpha-ketoglutarate-dependent mitochondrial dioxygenase. | Hulse JD, Ellis SR, Henderson LM | 1978 Mar 10 | 627563 |
| Molecular and Biochemical Characterization of Rat epsilon -N-Trimethyllysine Hydroxylase, the First Enzyme of Carnitine Biosynthesis. | Vaz FM, Ofman R, Westinga K, Back JW, Wanders RJ | 2001 Sep 7 | 11431483 |
| Evidence That Trimethyllysine Hydroxylase Catalyzes the Formation of (2S,3S)-3-Hydroxy-N<sup>ε</sup>-trimethyllysine. | Reddy YV, Al Temimi AH, White PB, Mecinović J | 2017 Jan 20 | 28045275 |
| Human carnitine biosynthesis proceeds via (2S,3S)-3-hydroxy-N<sup>ε</sup>-trimethyllysine. | Leśniak RK, Markolovic S, Tars K, Schofield CJ | 2016 Dec 22 | 27965989 |
| Substrate scope for trimethyllysine hydroxylase catalysis. | Al Temimi AH, Pieters BJ, Reddy YV, White PB, Mecinović J | 2016 Oct 25 | 27730239 |