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Information on EC 1.14.11.1 - gamma-butyrobetaine dioxygenase and Organism(s) Rattus norvegicus and UniProt Accession Q9QZU7

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IUBMB Comments
Requires Fe2+ and ascorbate.
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This record set is specific for:
Rattus norvegicus
UNIPROT: Q9QZU7
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Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
gamma-butyrobetaine hydroxylase, bbox1, butyrobetaine hydroxylase, gamma-butyrobetaine dioxygenase, gamma-butyrobetaine hydroxylase 1, alpha-butyrobetaine hydroxylase, bu hydroxylase, gbb hydroxylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
gamma-butyrobetaine hydroxylase
-
alpha-butyrobetaine hydroxylase
-
-
-
-
Bu hydroxylase
-
-
butyrobetaine hydroxylase
-
-
-
-
gamma butyrobetaine hydroxylase
-
-
gamma-buryrobetaine dioxygenase
-
-
gamma-butyrobetaine hydroxylase
GBB hydroxylase
-
-
oxygenase, gamma-butyrobetaine di-
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
oxidative decarboxylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
4-trimethylammoniobutanoate,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
Requires Fe2+ and ascorbate.
CAS REGISTRY NUMBER
COMMENTARY hide
9045-31-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-trimethylaminopropionic acid + 2-oxoglutarate + O2
?
show the reaction diagram
-
20% of the hydroxylation rate of gamma-butyrobetaine
-
-
?
4-dimethylaminobutyric acid + 2-oxoglutarate + O2
4-dimethylamino-3-hydroxybutyric acid + succinate + CO2
show the reaction diagram
4-trimethylammoniobutanoate + 2-oxoglutarate + O2
3-hydroxy-4-trimethylammoniobutanoate + succinate + CO2
show the reaction diagram
D-carnitine + 2-oxoglutarate + O2
3-carboxy-N,N,N-trimethyl-2-oxopropan-1-aminium + succinate + CO2
show the reaction diagram
-
-
-
-
r
L-carnitine + 2-oxoglutarate + O2
3-carboxy-N,N,N-trimethyl-2-oxopropan-1-aminium + succinate + CO2
show the reaction diagram
-
-
-
-
r
additional information
?
-
enzyme is involved in L-carnitine (3-hydroxy-4-N-trimethylaminobutyrate) biosynthesis
-
-
?
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
additional information
?
-
enzyme is involved in L-carnitine (3-hydroxy-4-N-trimethylaminobutyrate) biosynthesis
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,6-dichlorophenolindophenol
-
-
ascorbate
additional information
-
KCl, nicotinamide, MgCl2 or catalase not required for full activity
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxoglutarate
-
at concentrations above 1 mM
3-(2,2,2-trimethylhydrazinium)propionate
-
complete inhibition at 0.05 mM
3-(2,2,2-trimethylhydrazinium)propionate dihydrate
-
-
3-Bromo-2-oxoglutarate
-
noncompetitive inhibition, 2-oxoglutarate as variable substrate
3-glutathione-2-oxoglutarate
-
noncompetitive to 2-oxoglutarate
3-trimethylaminopropyl-1-sulfonate
-
-
arsenite
-
-
ascorbate
-
-
DL-carnitine
-
-
FMN
-
in high concentrations
gamma-butyrobetaine
-
at concentrations above 0.2 mM
iodoacetate
-
less effective than p-chloromercuriphenylsulfonate
Iodosobenzoate
-
less effective than p-chloromercuriphenylsulfonate
N-ethylmaleimide
-
less effective than p-chloromercuriphenylsulfonate
p-aminomethylbenzoic acid
-
1.2 mmol/kg reduces the conversion of 4-dimethylaminobutyric acid to 4-dimethylamino-3-hydroxybutyric acid from 62.6% to 46.8%
p-chloromercuribenzoate
-
inactivates enzyme completely at 0.1 mM
p-chloromercuriphenylsulfonate
-
inactivates enzyme completely at 0.1 mM
phosphate
-
-
Quinacrine
-
-
structure analogues of gamma-butyrobetaine and 2-oxoglutarate
-
-
-
Succinic semialdehyde
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-amino-6,7-dimethyl-4-hydroxy-5,6,7,8-tetrahydropteridine
-
-
catalase
-
Cs+
-
increase of activity
GSH/GSH-peroxidase
-
increase of activity, more efficient in assay and during preincubation than catalase, protects the enzyme from increasing phosphate concentrations
-
isoascorbate
-
increase of activity
K+
-
efficient coupling of decarboxylation and hydroxylation, stimulation
Microsomal preparation
-
increase of activity
-
NADPH
-
NADPH-regenerating system, increase of activity, no absolute requirement
NH4+
-
increase of activity
nicotinamide
-
increase of activity
Rb+
-
increase of activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.125
2-oxo-glutarate
-
-
0.5
2-oxoglutarate
-
-
0.47
D-carnitine
-
-
0.029 - 0.08
gamma-butyrobetaine
0.052
L-carnitine
-
-
additional information
additional information
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7.5
-
half-maximal activity at pH 6.0 and 7.5
6 - 8.4
-
half-maximal activity at pH 6.0 and 8.4, partially purified preparation
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
the enzyme is expressed but without activity in renal tissue
Manually annotated by BRENDA team
additional information
-
no activity found: muscle, kidney
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
biosynthesis of carnitine, important role in beta-oxidation of fatty acid
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
BODG_RAT
387
0
44546
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43000
-
2 * 43000, SDS-PAGE
44000
-
x * 44000, SDS-PAGE
68000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 44000, SDS-PAGE
dimer
-
2 * 43000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
-
complete inactivation after 15 min
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
O2, irreversible inactivation during preincubation
-
439297
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 50 mM sodium phosphate pH 7.4, 20 mM KCl, 10 mM DTT, 200g/l glycerol are best conservation conditions
-
addition of EDTA causes total loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in HEK293 cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
detection of mRNA levels during suckling period onwards, expression is ontogenically regulated
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
effects of hyperthyroidism and hypothyroidism on enzyme activity
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lindstedt, G.; Lindstedt, S.
Cofactor requirements of gamma-butyrobetaine hydroxylase from rat liver
J. Biol. Chem.
245
4178-4186
1970
Rattus norvegicus
Manually annotated by BRENDA team
Carter, A.L.; Stratman, F.W.
A rapid and sensitive assay of gamma-butyrobetaine hydroxylase
FEBS Lett.
111
112-114
1980
Rattus norvegicus
Manually annotated by BRENDA team
Punekar, N.S.; Wehbie, R.S.; Lardy, H.A.
gamma-Butyrobetaine hydroxylase and the protective role of glutathione peroxidase
J. Biol. Chem.
262
6720-6724
1987
Rattus norvegicus
Manually annotated by BRENDA team
Wehbie, R.S.; Punekar, N.S.; Lardy, H.A.
Rat liver gamma-butyrobetaine hydroxylase catalyzed reaction: influence of potassium, substrates, and substrate analogues on hydroxylation and decarboxylation
Biochemistry
27
2222-2228
1988
Rattus norvegicus
Manually annotated by BRENDA team
Lindstedt, G.
Hydroxylation of gamma-butyrobetaine to carnitine in rat liver
Biochemistry
6
1271-1282
1967
Rattus norvegicus
Manually annotated by BRENDA team
Paul, H.S.; Sekas, G.; Adibi, S.A.
Carnitine biosynthesis in hepatic peroxisomes. Demonstration of gamma-butyrobetaine hydroxylase activity
Eur. J. Biochem.
203
599-605
1992
Rattus norvegicus
Manually annotated by BRENDA team
Vaz, F.M.; van Gool, S.; Ofman, R.; Ijlst, L.; Wanders, R.J.
Carnitine biosynthesis. Purification of gamma-butyrobetaine hydroxylase from rat liver
Adv. Exp. Med. Biol.
466
117-124
1999
Rattus norvegicus
Manually annotated by BRENDA team
Galland, S.; Le Borgne, F.; Guyonnet, D.; Clouet, P.; Demarquoy, J.
Purification and characterization of the rat liver gamma-butyrobetaine hydroxylase
Mol. Cell. Biochem.
178
163-168
1998
Rattus norvegicus
Manually annotated by BRENDA team
Galland, S.; Georges, B.; Le Borgne, F.; Conductier, G.; Dias, J.V.; Demarquoy, J.
Thyroid hormone controls carnitine status through modifications of g-butyrobetaine hydroxylase activity and gene expression
Cell. Mol. Life Sci.
59
540-545
2002
Rattus norvegicus
Manually annotated by BRENDA team
Galland, S.; Le Borgne, F.; Bouchard, F.; Georges, B.; Clouet, P.; Grand-Jean, F.; Demarquoy, J.
Molecular cloning and characterization of the cDNA encoding the rat liver gamma-butyrobetaine hydroxylase
Biochim. Biophys. Acta
1441
85-92
1999
Rattus norvegicus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Debreceni, B.; Farkas, V.; Fischer, G.M.; Sandor, A.
Effect of aromatic ring-containing drugs on carnitine biosynthesis in rats with special regard to p-aminomethylbenzoic acid
Metab. Clin. Exp.
54
1582-1586
2005
Rattus norvegicus
Manually annotated by BRENDA team
Buermans, H.P.; Redout, E.M.; Schiel, A.E.; Musters, R.J.; Zuidwijk, M.; Eijk, P.P.; van Hardeveld, C.; Kasanmoentalib, S.; Visser, F.C.; Ylstra, B.; Simonides, W.S.
Microarray analysis reveals pivotal divergent mRNA expression profiles early in the development of either compensated ventricular hypertrophy or heart failure
Physiol. Genomics
21
314-323
2005
Rattus norvegicus
Manually annotated by BRENDA team
Fujita, M.; Nakanishi, T.; Shibue, Y.; Kobayashi, D.; Moseley, R.H.; Shirasaka, Y.; Tamai, I.
Hepatic uptake of gamma-butyrobetaine, a precursor of carnitine biosynthesis, in rats
Am. J. Physiol. Gastrointest. Liver Physiol.
297
G681-G686
2009
Rattus norvegicus
Manually annotated by BRENDA team
Garcia-Delgado, M.; Peral, M.J.; Duran, J.M.; Garcia-Miranda, P.; Calonge, M.L.; Ilundain, A.A.
Ontogeny of Na(+)/L-carnitine transporter and of gamma-trimethylaminobutyraldehyde dehydrogenase and gamma-butyrobetaine hydroxylase genes expression in rat kidney
Mech. Ageing Dev.
130
227-233
2009
Rattus norvegicus (Q9QZU7)
Manually annotated by BRENDA team