Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli BL21-AI cells | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
D244E | the Km-value of the variant enzyme for N6,N6,N6-trimethyl-L-lysine is 3.7fold lower than the Km-value of the wild-type enzyme, the Km-value of the variant enzyme for 2-oxoglutarate is 2.7fold higher than the Km-value of the wild-type enzyme | Homo sapiens |
T269A | the Thr269Ala variant displays high enzymatic activity (96% at 0.10 mM, 76% at 0.003 mM) for the conversion of (2S)-Nepsilon-trimethyllysine to (2S,3S)-3-hydroxy-Nepsilon-trimethyllysine | Homo sapiens |
W221F | the variant displays considerably reduced enzymatic activity (32%), implying that the OH group of Tyr404 contributes to stronger interaction with the trimethylammonium group of (2S)-Nepsilon-trimethyllysine | Homo sapiens |
Y217D | the variants does not display any enzymatic activity within limits of detection | Homo sapiens |
Y217E | the Thr269Ala variant displays high enzymatic activity (96% at 0.10 mM, 76% at 0.003 mM) for the conversion of (2S)-Nepsilon-trimethyllysine to (2S,3S)-3-hydroxy-Ne-trimethyllysine | Homo sapiens |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.32 | - |
N6,N6,N6-Trimethyl-L-lysine | mutant enzyme D244E, pH 7.5, 37°C | Homo sapiens | |
0.35 | - |
2-oxoglutarate | mutant enzyme W221F, pH 7.5, 37°C | Homo sapiens | |
0.42 | - |
2-oxoglutarate | wild-type enzyme, pH 7.5, 37°C | Homo sapiens | |
0.7 | - |
N6,N6,N6-Trimethyl-L-lysine | mutant enzyme T269A, pH 7.5, 37°C | Homo sapiens | |
1.12 | - |
2-oxoglutarate | mutant enzyme D244E, pH 7.5, 37°C | Homo sapiens | |
1.18 | - |
N6,N6,N6-Trimethyl-L-lysine | wild-type enzyme, pH 7.5, 37°C | Homo sapiens | |
1.47 | - |
N6,N6,N6-Trimethyl-L-lysine | mutant enzyme W221F, pH 7.5, 37°C | Homo sapiens | |
1.97 | - |
2-oxoglutarate | mutant enzyme T269A, pH 7.5, 37°C | Homo sapiens |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | non-heme Fe(II)-dependent oxygenase | 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 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Homo sapiens |
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 | recognition sites that contribute to the enzymatic activity of the enzyme (TMLH): the Fe(II)-binding H242-D244-H389 residues, R391-R398 involved in 2-oxoglutarate-binding, and several residues (D231, N334, and the aromatic cage comprised of W221, Y217 and Y234) associated with binding of (2S)-Nepsilon-trimethyllysine | Homo sapiens | (3S)-3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
TMLH | - |
Homo sapiens |
trimethyllysine hydroxylase | - |
Homo sapiens |
General Information | Comment | Organism |
---|---|---|
physiological function | the enzyme catalyzes the first step in carnitine biosynthesis | Homo sapiens |