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Literature summary for 1.14.11.8 extracted from

  • Wang, Y.; Vijayendar Reddy, Y.; Al Temimi, A.; Venselaar, H.; Nelissen, F.; Lenstra, D.; Mecinovic, J.
    Investigating the active site of human trimethyllysine hydroxylase (2019), Biochem. J., 476, 1109-1119 .
    View publication on PubMed
Search for more literature for 1.14.11.8

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21-AI cells Homo sapiens

Protein Variants

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 [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

Metals/Ions Comment Organism Structure
Fe2+ non-heme Fe(II)-dependent oxygenase Homo sapiens

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Homo sapiens Q9NVH6
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Homo sapiens

Substrates and Products (Substrate)

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

Synonyms Comment Organism
TMLH
-
 Homo sapiens
trimethyllysine hydroxylase
-
 Homo sapiens

General Information

General Information Comment Organism
physiological function the enzyme catalyzes the first step in carnitine biosynthesis Homo sapiens