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Enzyme Nomenclature
Information on EC 1.14.11.8 - trimethyllysine dioxygenase
for references in articles please use BRENDA:EC1.14.11.8
Word Map on EC 1.14.11.8
- 1.14.11.8
- carnitine
- gamma-butyrobetaine
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long-chain
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autism
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inborn
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hydroxymethyltransferase
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Specify your search results
The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.14.11.8
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RECOMMENDED NAME
GeneOntology No.
trimethyllysine dioxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2 = 3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
N6,N6,N6-trimethyl-L-lysine,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
Requires Fe2+ and ascorbate.
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CAS REGISTRY NUMBER
COMMENTARY
84012-77-1
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
metabolism
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the enzyme catalyzes the first step in the biosynthesis of carnitine
metabolism
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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
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2
3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
additional information
?
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enzyme is localized to the mitochondrial matrix, product formation is limited by 6-N-trimethyllysine transport across the mitochondrial inner membrane
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N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2
3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
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N6,N6, N6-trimethyl-L-lysine is epsilon-N-trimethyl-L-lysine
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-
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N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2
3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
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-
-
-
?
N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2
3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
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-
?
N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2
3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
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-
-
-
?
N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2
3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
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-
-
?
N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2
3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
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N6,N6, N6-trimethyl-L-lysine is epsilon-N-trimethyl-L-lysine
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-
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N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2
3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
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-
-
-
?
N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2
3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
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-
?
N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2
3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
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N6,N6, N6-trimethyl-L-lysine is epsilon-N-trimethyl-L-lysine
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N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2
3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
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N6,N6, N6-trimethyl-L-lysine is epsilon-N-trimethyl-L-lysine
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-
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N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2
3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
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carnitine biosynthesis
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N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2
3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
first enzyme of the L-carnitine biosynthesis
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?
N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2
3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
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?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2
3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
additional information
?
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-
enzyme is localized to the mitochondrial matrix, product formation is limited by 6-N-trimethyllysine transport across the mitochondrial inner membrane
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N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2
3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
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-
-
-
?
N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2
3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
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carnitine biosynthesis
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N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2
3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
Q91ZW6
first enzyme of the L-carnitine biosynthesis
-
?
N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2
3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
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-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Fe2+
Fe2+
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preincubation with Fe2+ in absence of other cofactors inactivates (ascorbate or dithiothreitol prevents inactivation); required
Fe2+
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absence of the cofactor Fe2+ does not completely abolish enzyme activity, even when endogenous Fe2+ is removed from the homogenate with a gel filtration column
Fe2+
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absence of the cofactor Fe2+ does not completely abolish enzyme activity, even when endogenous Fe2+ is removed from the homogenate with a gel filtration column
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
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tissue-dependent enzyme expression in case of high-lysine diet, overview
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
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no activity found in microsomal or soluble fractions of liver
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mitochondrial matrix, product formation is limited by 6-N-trimethyllysine transport across the mitochondrial inner membrane
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
the enzyme is synthesized as a 47500 Da precursor and processed to a mature protein of 43000 Da, presumably upon import into mitochondria
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in COS-1 cells
when the putative cDNA is expressed in either Escherichia coli or Saccharomyces cerevisiae no enzyme activity can be detected in lysates of theses cells. High activity can be measured in lysates of COS cells transfected with the putative rat cDNA, whereas only low activity is measured in lysates of cells transfected with the pcDNA3 vector without insert
when the putative cDNA is expressed in either Escherichia coli or Saccharomyces cerevisiae no enzyme activity can be detected in lysates of theses cells. High activity can be measured in lysates of COS cells transfected with the putative rat cDNA, whereas only low activity is measured in lysates of cells transfected with the pcDNA3 vector without insert
when the putative cDNA is expressed in either Escherichia coli or Saccharomyces cerevisiae no enzyme activity can be detected in lysates of theses cells. High activity can be measured in lysates of COS cells transfected with the putative rat cDNA, whereas only low activity is measured in lysates of cells transfected with the pcDNA3 vector without insert
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H389L
additional information
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construction of senescence marker protein-30/gluconolactonase knockout mice, which cannot synthesize L-ascorbate in vivo, the mutant mice nevertheless produce normal levels of carnitine when fed an L-ascorbate lacking diet
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.11.8)
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