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Literature summary for 1.14.11.8 extracted from

  • Fischer, M.; Hirche, F.; Kluge, H.; Eder, K.
    A moderate excess of dietary lysine lowers plasma and tissue carnitine concentrations in pigs (2009), Br. J. Nutr., 101, 190-196.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
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Sus scrofa 5739
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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 Sus scrofa
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3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
-
?

Organism

Organism UniProt Comment Textmining
Sus scrofa
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male crossbred pigs, German Landrace x Large White x Pietrain
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Source Tissue

Source Tissue Comment Organism Textmining
kidney
-
Sus scrofa
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liver
-
Sus scrofa
-
additional information tissue-dependent enzyme expression in case of high-lysine diet, overview Sus scrofa
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skeletal muscle musculus longissimus dorsi and musculus semimembranosus Sus scrofa
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2
-
Sus scrofa 3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
-
?

Synonyms

Synonyms Comment Organism
TML dioxygenase
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Sus scrofa
TMLD
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Sus scrofa

Expression

Organism Comment Expression
Sus scrofa pigs fed a high-lysine diet have lower concentrations of free and total carnitine in plasma, liver, kidney and skeletal muscle than control pigs, and have an increased concentration of trimethyllysine, TML, a reduced mRNA abundance of TML dioxygenase and reduced concentrations of gamma-butyrobetaine in muscle, indicating that the conversion of trimethyllysine into gamma-butyrobetaine in muscle is impaired down

General Information

General Information Comment Organism
metabolism the enzyme catalyzes the first step in the biosynthesis of carnitine, i.e. L-3-hydroxy-4-N-N-N-trimethylaminobutyrate. Lysine in protein peptide linkages undergoes methylation of the 1-amino group to yield trimethyllysine, TML, which is released upon protein degradation. Muscle is the major source of TML. The released TML is further oxidised to gamma-butyrobetaine by the action of trimethyllysine dioxygenase, 3-hydroxy-N-trimethyllysine aldolase and 4-N-trimethylaminobutyraldehyde dehydrogenase Sus scrofa