Information on EC 1.14.11.8 - trimethyllysine dioxygenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.11.8
-
RECOMMENDED NAME
GeneOntology No.
trimethyllysine dioxygenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2 = 3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-carnitine biosynthesis
-
-
Lysine degradation
-
-
carnitine metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
N6,N6,N6-trimethyl-L-lysine,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
Requires Fe2+ and ascorbate.
CAS REGISTRY NUMBER
COMMENTARY hide
84012-77-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
male crossbred pigs, German Landrace x Large White x Pietrain
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
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
show the reaction diagram
additional information
?
-
-
enzyme is localized to the mitochondrial matrix, product formation is limited by 6-N-trimethyllysine transport across the mitochondrial inner membrane
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
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
show the reaction diagram
additional information
?
-
-
enzyme is localized to the mitochondrial matrix, product formation is limited by 6-N-trimethyllysine transport across the mitochondrial inner membrane
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
FeSO4
-
required
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
alpha-N-Acetyltrimethyllysine
-
-
citrate
-
-
Hydroxytrimethyllysine
-
4 stereoisomers
isocitrate
-
-
Lactate
-
-
malonate
-
-
p-chloromercuribenzoate
-
-
succinate
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxoglutarate
dithiothreitol
-
sparing as well as augmenting effect
L-ascorbic acid
-
activates, but is not essentially required
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.109 - 0.133
2-oxoglutarate
0.22
alpha-ketoglutarate
-
-
0.13 - 1.1
N6,N6,N6-Trimethyl-L-lysine
1.6
trimethyllysine
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7.5
at 37°C
6.8
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
musculus longissimus dorsi and musculus semimembranosus
Manually annotated by BRENDA team
additional information
-
tissue-dependent enzyme expression in case of high-lysine diet, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
no activity found in microsomal or soluble fractions of liver
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43000
2 * 43000, calculation from nucleotide sequence
52000
-
x * 52000 + x * 65000, SDS-PAGE
65000
-
x * 52000 + x * 65000, SDS-PAGE
87000
gel filtration, non-denaturing PAGE
180000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 52000 + x * 65000, SDS-PAGE
dimer
2 * 43000, calculation from nucleotide sequence
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0
-
half-life: 5 days
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0°C, half-life: 5 days
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial
-
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
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
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
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