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Information on EC 1.14.11.8 - trimethyllysine dioxygenase
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1.14.11.8 trimethyllysine dioxygenaseIUBMB Comments
Requires Fe2+ and ascorbate.
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Word Map
- 1.14.11.8
- carnitine
- gamma-butyrobetaine
-
autism
-
inborn
- aldolase
-
transporter-2
-
proliferator-activated
- hydroxymethyltransferase
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
6-N-trimethyllysine dioxygenase, epsilon-N-trimethyllysine hydroxylase, epsilon-trimethyllysine 2-oxoglutarate dioxygenase, eta-N-trimethyllysine hydroxylase, Nepsilon-trimethyllysine hydroxylase, oxygenase, trimethyllysine di-, TML dioxygenase, TML hydroxylase, TML-alpha-ketoglutarate dioxygenase, TMLD, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
6-N-trimethyllysine dioxygenase
epsilon-N-trimethyllysine hydroxylase
epsilon-trimethyllysine 2-oxoglutarate dioxygenase
-
-
-
-
eta-N-trimethyllysine hydroxylase
oxygenase, trimethyllysine di-
-
-
-
-
TML dioxygenase
TML hydroxylase
-
-
-
-
TML-alpha-ketoglutarate dioxygenase
-
-
-
-
TMLD
TMLH
TMLH-a
TMLH-b
trimethyllysine alpha-ketoglutarate dioxygenase
-
-
-
-
trimethyllysine hydroxylase
TML dioxygenase
-
-
-
-
TMLD
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2 = (3S)-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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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
MetaCyc
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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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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
N5,N5,N5-trimethyl-L-ornithine + 2-oxoglutarate + O2
(3S)-3-hydroxy-N5,N5,N5-trimethyl-L-ornithine + succinate + CO2
-
-
-
-
?
N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2
(3S)-3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2
3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
N6,N6-dimethyl-N6-ethyl-L-lysine + 2-oxoglutarate + O2
(3S)-3-hydroxy-N6,N6-dimethyl-N6-ethyl-L-lysine + succinate + CO2
-
-
-
-
?
N6,N6-dimethyl-N6-isopropyl-L-lysine + 2-oxoglutarate + O2
(3S)-3-hydroxy-N6,N6-dimethyl-N6-isopropyl-L-lysine + succinate + CO2
-
-
-
-
?
N6,N6-dimethyl-N6-propyl-L-lysine + 2-oxoglutarate + O2
(3S)-3-hydroxy-N6,N6-dimethyl-N6-propyl-L-lysine + succinate + CO2
-
-
-
-
?
N6-fluoromethyl-N6,N6-dimethyl-L-lysine + 2-oxoglutarate + O2
(3S)-3-hydroxy-N6-fluoromethyl-N6,N6-dimethyl-L-lysine + succinate + CO2
-
Nepsilon-trimethyllysine analogue that contains the fluoromethyl group can be used as a 1H and 19F NMR probe for studies on TMLH catalysis
-
-
?
N7,N7,N7-trimethyl-L-alpha-homolysine + 2-oxoglutarate + O2
(3S)-3-hydroxy-N7,N7,N7-trimethyl-L-alpha-homolysine + succinate + CO2
-
-
-
-
?
N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2
(3S)-3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
-
-
-
-
?
N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2
(3S)-3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
-
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
-
-
?
N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2
3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
-
N6,N6, N6-trimethyl-L-lysine is epsilon-N-trimethyl-L-lysine
-
-
-
N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2
3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
-
-
-
-
?
N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2
3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
-
-
?
N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2
3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
-
-
-
-
?
N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2
3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
-
-
-
?
N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2
3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
-
N6,N6, N6-trimethyl-L-lysine is epsilon-N-trimethyl-L-lysine
-
-
-
N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2
3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
-
-
-
-
?
N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2
3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
-
-
?
N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2
3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
-
N6,N6, N6-trimethyl-L-lysine is epsilon-N-trimethyl-L-lysine
-
-
N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2
3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
-
N6,N6, N6-trimethyl-L-lysine is epsilon-N-trimethyl-L-lysine
-
-
-
N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2
3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
-
carnitine biosynthesis
-
-
-
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
-
?
N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2
3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
-
-
-
-
?
additional information
?
-
-
determination of the (2S,3S)-3-hydroxy-N6,N6,N6-trimethyl-L-lysine and N6,N6,N6-trimethyl-L-lysine is performed by ultraperformance liquid chromatography–tandem mass spectrometry (UPLC/MS/MS) in positive ion electrospray mode
-
-
-
additional information
?
-
-
NMR spectrosopic structure analysis of substrates and products
-
-
-
additional information
?
-
-
NMR spectrosopic structure analysis of substrates and products, substrate specificity, overview. No or poor activity with dimethyllysine, methyllysine, lysine, D-trimethyllysine, 5-trimethylamino-1-aminopentane, trimethyllysine, 6-trimethylaminohexanoic acid, hexamethyllysine, N-acetyltrimethyllysine, trimethyldiaminobutyric acid, triethyllysine, symmetric and asymmetric dimethylarginines, mildronate, and gamma-butyrobetaine, structure-activity relationship study
-
-
-
additional information
?
-
-
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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NATURAL SUBSTRATE
NATURAL 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
(3S)-3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
-
-
-
-
?
N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2
3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
additional information
?
-
-
enzyme is localized to the mitochondrial matrix, product formation is limited by 6-N-trimethyllysine transport across the mitochondrial inner membrane
-
-
-
N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2
3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
-
-
-
-
?
N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2
3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
-
carnitine biosynthesis
-
-
-
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
-
?
N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2
3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Fe2+
Fe2+
-
preincubation with Fe2+ in absence of other cofactors inactivates (ascorbate or dithiothreitol prevents inactivation); required
Fe2+
-
dependent on, non-heme Fe(II) and 2-oxoglutarate dependent oxygenase, Fe2+ is required for catalysis
Fe2+
-
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+
-
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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INHIBITOR
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
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
tissue-dependent enzyme expression in case of high-lysine diet, overview
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
no activity found in microsomal or soluble fractions of liver
-
brenda
-
mitochondrial matrix, product formation is limited by 6-N-trimethyllysine transport across the mitochondrial inner membrane
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
-
residue Asp131 in TMLHis responsible for specific binding of the alpha-ammonium group of trimethyllysine
evolution
-
the enzyme belongs to the non-heme Fe(II) and 2-oxoglutarate dependent oxygenases
evolution
-
the enzyme belongs to the family of 2-oxoglutarate (2OG)-dependent oxygenases
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
metabolism
-
the enzyme catalyzes the first step in the biosynthesis of carnitine
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
metabolism
-
trimethyllysine hydroxylase (TMLH) catalyses C-3 hydroxylation of Nepsilon-trimethyllysine in the first step of carnitine biosynthesis
metabolism
-
the enzyme catalyses the first step in mammalian biosynthesis of carnitine, which plays a crucial role in fatty acid metabolism. Carnitine biosynthesis patway, overview
metabolism
-
trimethyllysine hydroxylase (TMLH) catalyses C-3 hydroxylation of Nepsilon-trimethyllysine in the first step of carnitine biosynthesis in humans
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
metabolism
-
trimethyllysine hydroxylase (TMLH) catalyses the first step in carnitine biosynthesis, the conversion of N6,N6,N6-trimethyl-L-lysine to 3-hydroxy-N6,N6,N6-trimethyl-L-lysine
physiological function
-
trimethyllysine hydroxylase (TMLH) catalyses C-3 hydroxylation of Nepsilon-trimethyllysine in the first step of carnitine biosynthesis
physiological function
-
trimethyllysine hydroxylase (TMLH) catalyses C-3 hydroxylation of Nepsilon-trimethyllysine in the first step of carnitine biosynthesis in humans
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
TMLH_NEUCR
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
471
0
52630
Swiss-Prot
TMLH_PICGU
Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324)
399
0
46267
Swiss-Prot
A0A0F8B130_CERFI
449
0
50479
TrEMBL
K0KN74_WICCF
Wickerhamomyces ciferrii (strain F-60-10 / ATCC 14091 / CBS 111 / JCM 3599 / NBRC 0793 / NRRL Y-1031)
457
0
53219
TrEMBL
A0A3R7UTV3_9PROT
374
0
43439
TrEMBL
B8M6P7_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
536
0
61176
TrEMBL
M5BUN9_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
213
0
24153
TrEMBL
K0KSH8_WICCF
Wickerhamomyces ciferrii (strain F-60-10 / ATCC 14091 / CBS 111 / JCM 3599 / NBRC 0793 / NRRL Y-1031)
345
0
40599
TrEMBL
A0A075B0I0_ROZAC
Rozella allomycis (strain CSF55)
318
0
37521
TrEMBL
A0A424RXC6_9PROT
365
0
42513
TrEMBL
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H389L
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
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, recombinant enzyme, after storage at 4°C for 4 days, MBP-TMLH retains 96% of its activity, while detagged TMLH shows only 77% activity compared to fresh enzyme preparation
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant active and stable His- and MBP-tagged TMLH from Escherichia coli strain BL21-AI by nickel or amylose affinity chromatography. It is possible that the His6-tag at the N-terminus of the fusion protein is masked and cannot be accessed by the Ni-beads. Thus, MBP affinity purification is selected as a first purification step, followed by gel filtration, His6-MBP-tag cleavage by recombinant TEV protease
-
recombinant MBP-taged enzyme by affinity chromatography, tag cleavage by rTEV protease, and gel filtration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in COS-1 cells
gene TMLH, recombinant overexpression of active and stable TMLH as a His-tagged maltose-binding protein fusion in Escherichia coli strain BL21-AI. Coexpression of the enzyme with chaperones GroES/EL increases the expression level by one order of magnitude
-
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hulse, J.D.; Ellis, S.R.; Henderson, L.M.
Carnitine biosynthesis. beta-Hydroxylation of trimethyllysine by an alpha-ketoglutarate-dependent mitochondrial dioxygenase
J. Biol. Chem.
253
1654-1659
1978
Rattus norvegicus
brenda
Henderson, L.M.; Nelson, P.J.; Henderson, L.
Mammalian enzymes of trimethyllysine conversion to trimethylaminobutyrate
Fed. Proc.
41
2843-2847
1982
Bos taurus
brenda
Sachan, D.S.; Hoppel, C.L.
Carnitine biosynthesis. Hydroxylation of N6-trimethyl-lysine to 3-hydroxy-N6-trimethyl-lysine
Biochem. J.
188
529-534
1980
Rattus norvegicus
brenda
Sachan, D.S.; Broquist, H.P.
Synthesis of carnitine from epsilon-N-trimethyllysine in post mitochondrial fractions of Neurospora crassa
Biochem. Biophys. Res. Commun.
96
870-875
1980
Neurospora crassa
brenda
Swiegers, J.H.; Vaz, F.M.; Pretorius, I.S.; Wanders, R.J.A.; Bauer, F.F.
Carnitine biosynthesis in neurospora crassa: identification of a cDNA coding for epsilon-N-trimethyllysine hydroxylase and its functional expression in Saccharomyces cerevisiae
FEMS Microbiol. Lett.
210
19-23
2002
Neurospora crassa
brenda
Vaz, F.M.; Ofman, R.; Westinga, K.; Back, J.W.; Wanders, R.J.A.
Molecular and biochemical characterization of rat epsilon-N-trimethyllysine hydroxylase, the first enzyme of carnitine biosynthesis
J. Biol. Chem.
276
33512-33517
2001
Homo sapiens, Homo sapiens (Q9NVH6), Mus musculus, Mus musculus (Q91ZE0), Rattus norvegicus (Q91ZW6)
brenda
van Vlies, N.; Wanders, R.J.; Vaz, F.M.
Measurement of carnitine biosynthesis enzyme activities by tandem mass spectrometry: differences between the mouse and the rat
Anal. Biochem.
354
132-139
2006
Mus musculus, Rattus norvegicus
brenda
Monfregola, J.; Cevenini, A.; Terracciano, A.; van Vlies, N.; Arbucci, S.; Wanders, R.J.; DUrso, M.; Vaz, F.M.; Ursini, M.V.
Functional analysis of TMLH variants and definition of domains required for catalytic activity and mitochondrial targeting
J. Cell. Physiol.
204
839-847
2005
Homo sapiens, Mus musculus
brenda
Davis, A.T.; Monroe, T.J.
Carnitine deficiency and supplementation do not affect the gene expression of carnitine biosynthetic enzymes in rats
J. Nutr.
135
761-764
2005
Rattus norvegicus
brenda
van Vlies, N.; Ofman, R.; Wanders, R.J.; Vaz, F.M.
Submitochondrial localization of 6-N-trimethyllysine dioxygenase - implications for carnitine biosynthesis
FEBS J.
274
5845-5851
2007
Rattus norvegicus
brenda
Furusawa, H.; Sato, Y.; Tanaka, Y.; Inai, Y.; Amano, A.; Iwama, M.; Kondo, Y.; Handa, S.; Murata, A.; Nishikimi, M.; Goto, S.; Maruyama, N.; Takahashi, R.; Ishigami, A.
Vitamin C is not essential for carnitine biosynthesis in vivo: verification in vitamin C-depleted senescence marker protein-30/gluconolactonase knockout mice
Biol. Pharm. Bull.
31
1673-1679
2008
Mus musculus (Q91ZE0)
brenda
Fischer, M.; Hirche, F.; Kluge, H.; Eder, K.
A moderate excess of dietary lysine lowers plasma and tissue carnitine concentrations in pigs
Br. J. Nutr.
101
190-196
2009
Sus scrofa
brenda
Al Temimi, A.H.; Pieters, B.J.; Reddy, Y.V.; White, P.B.; Mecinovic, J.
Substrate scope for trimethyllysine hydroxylase catalysis
Chem. Commun. (Camb.)
52
12849-12852
2016
Homo sapiens, Homo sapiens (Q9NVH6)
brenda
Lesniak, R.; Markolovic, S.; Tars, K.; Schofield, C.
Human carnitine biosynthesis proceeds via (2S,3S)-3-hydroxy-Nepsilon-trimethyllysine
Chem. Commun. (Camb.)
53
440-442
2017
Homo sapiens (Q9NVH6)
brenda
Vijayendar Reddy, Y.; Al Temimi, A.H.; Mecinovic, J.
Fluorinated trimethyllysine as a (19)F NMR probe for trimethyllysine hydroxylase catalysis
Org. Biomol. Chem.
15
1350-1354
2017
Homo sapiens (Q9NVH6)
brenda
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
Org. Lett.
19
400-403
2017
Homo sapiens, Homo sapiens (Q9NVH6)
brenda
Kazaks, A.; Makrecka-Kuka, M.; Kuka, J.; Voronkova, T.; Akopjana, I.; Grinberga, S.; Pugovics, O.; Tars, K.
Expression and purification of active, stabilized trimethyllysine hydroxylase
Protein Expr. Purif.
104
1-6
2014
Homo sapiens (Q9NVH6)
brenda
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