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Literature summary for 1.14.11.8 extracted from

  • Reddy, Y.V.; Al Temimi, A.H.; White, P.B.; Mecinovi?, J.
    Evidence that trimethyllysine hydroxylase catalyzes the formation of (2S,3S)-3-hydroxy-N(epsilon)-trimethyllysine (2017), Org. Lett., 19, 400-403 .
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Homo sapiens 5739
-

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ dependent on, required for catalysis 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
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(3S)-3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q9NVH6
-
-

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 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

Synonyms Comment Organism
TMLH
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Homo sapiens
trimethyllysine hydroxylase
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Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Homo sapiens

General Information

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