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Information on EC 1.14.11.8 - trimethyllysine dioxygenase and Organism(s) Mus musculus and UniProt Accession Q91ZE0

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IUBMB Comments
Requires Fe2+ and ascorbate.
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This record set is specific for:
Mus musculus
UNIPROT: Q91ZE0
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
trimethyllysine hydroxylase, tmlh-b, epsilon-n-trimethyllysine hydroxylase, 6-n-trimethyllysine dioxygenase, tmlh-a, trimethyllysine dioxygenase, tml hydroxylase, tml dioxygenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6-N-trimethyllysine dioxygenase
-
6-N-trimethyllysine dioxygenase
-
-
epsilon-trimethyllysine 2-oxoglutarate dioxygenase
-
-
-
-
eta-N-trimethyllysine hydroxylase
-
-
oxygenase, trimethyllysine di-
-
-
-
-
TML dioxygenase
TML hydroxylase
-
-
-
-
TML-alpha-ketoglutarate dioxygenase
-
-
-
-
TMLH
-
-
TMLH-a
-
-
TMLH-b
-
-
trimethyllysine alpha-ketoglutarate dioxygenase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
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
-
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
-
-
-
?
N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2
3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL 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
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbate
-
10 mM
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Zn2+
-
1 mM, complete inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
L-ascorbic acid
activates, but is not essentially required
2-oxoglutarate
-
dependent
Fe2+
-
dependent
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the enzyme catalyzes the first step in the biosynthesis of carnitine
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TMLH_MOUSE
421
0
49610
Swiss-Prot
Mitochondrion (Reliability: 2)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H389L
-
enzyme not functional
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in COS-1 cells
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Mus musculus (Q91ZE0), Mus musculus, Rattus norvegicus (Q91ZW6), Homo sapiens (Q9NVH6), Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team