BRENDA - Enzyme Database show
show all sequences of 1.14.11.8

A moderate excess of dietary lysine lowers plasma and tissue carnitine concentrations in pigs

Fischer, M.; Hirche, F.; Kluge, H.; Eder, K.; Br. J. Nutr. 101, 190-196 (2009)

Data extracted from this reference:

Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
mitochondrion
-
Sus scrofa
5739
-
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2
Sus scrofa
-
3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Sus scrofa
-
male crossbred pigs, German Landrace x Large White x Pietrain
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
kidney
-
Sus scrofa
-
liver
-
Sus scrofa
-
additional information
tissue-dependent enzyme expression in case of high-lysine diet, overview
Sus scrofa
-
skeletal muscle
musculus longissimus dorsi and musculus semimembranosus
Sus scrofa
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2
-
697027
Sus scrofa
3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
-
-
-
?
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
mitochondrion
-
Sus scrofa
5739
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2
Sus scrofa
-
3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
-
-
?
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
kidney
-
Sus scrofa
-
liver
-
Sus scrofa
-
additional information
tissue-dependent enzyme expression in case of high-lysine diet, overview
Sus scrofa
-
skeletal muscle
musculus longissimus dorsi and musculus semimembranosus
Sus scrofa
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2
-
697027
Sus scrofa
3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
-
-
-
?
Expression
Organism
Commentary
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
Commentary
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
General Information (protein specific)
General Information
Commentary
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
Expression (protein specific)
Organism
Commentary
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
Other publictions for EC 1.14.11.8
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
744681
Lesniak
Human carnitine biosynthesis ...
Homo sapiens
Chem. Commun. (Camb.)
53
440-442
2017
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Vijayendar Reddy
Fluorinated trimethyllysine a ...
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15
1350-1354
2017
1
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745961
Reddy
Evidence that trimethyllysine ...
Homo sapiens
Org. Lett.
19
400-403
2017
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Al Temimi
Substrate scope for trimethyl ...
Homo sapiens
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2016
1
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7
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1
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1
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4
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Kazaks
Expression and purification o ...
Homo sapiens
Protein Expr. Purif.
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2014
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697027
Fischer
A moderate excess of dietary l ...
Sus scrofa
Br. J. Nutr.
101
190-196
2009
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1
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1
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1
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691166
Furusawa
Vitamin C is not essential for ...
Mus musculus
Biol. Pharm. Bull.
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1673-1679
2008
1
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1
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Submitochondrial localization ...
Rattus norvegicus
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Measurement of carnitine biosy ...
Mus musculus, Rattus norvegicus
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Functional analysis of TMLH va ...
Homo sapiens, Mus musculus
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13
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2
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675561
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Carnitine deficiency and suppl ...
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761-764
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651370
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