Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
mitochondrion | - |
Homo sapiens | 5739 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | dependent on, required for catalysis | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2 | Homo sapiens | - |
(3S)-3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | Q9NVH6 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2 | - |
Homo sapiens | (3S)-3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2 | - |
? | |
N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2 | the enzymatic hydroxylation occurs at the C-3 site of (2S)-Nepsilon-trimethyllysine substrate. Comparative NMR spectroscopic studies (with two enantiopure synthetic standards that possess 3R and 3S stereochemistry) on the enzymatically produced (2S)-3-hydroxy-Nepsilon-trimethyllysine reveal that TMLH exclusively catalyzes the formation of (3S)-3-hydroxy-Nepsilon-trimethyl-L-lysine, not forming any (3R)-3-hydroxy-Nepsilon-trimethyl-L-lysine diastereoisomer | Homo sapiens | (3S)-3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
TMLH | - |
Homo sapiens |
trimethyllysine hydroxylase | - |
Homo sapiens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Homo sapiens |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme belongs to the family of 2-oxoglutarate (2OG)-dependent oxygenases. Members of Fe(II) and 2-oxoglutarate-dependent oxygenases catalyze stereoselective hydroxylations of unactivated C-H bonds in various (bio)molecules, including proteins, DNA, and small molecule metabolites | Homo sapiens |
metabolism | trimethyllysine hydroxylase (TMLH) is involved in the first step of the physiologically important carnitine biosynthesis pathway. The enzyme catalyzes C-3 hydroxylation of (2S)-Nepsilon-L-trimethyllysine, to produce 3-hydroxy-Nepsilon-L-trimethyllysine, which then undergoes three additional enzymatic steps to the final L-carnitine | Homo sapiens |