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Information on EC 1.1.1.254 - (S)-carnitine 3-dehydrogenase
for references in articles please use BRENDA:EC1.1.1.254
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.254 (S)-carnitine 3-dehydrogenase
IUBMB Comments
Specific for the (S)-enantiomer of carnitine, i.e., the enantiomer of the substrate of EC 1.1.1.108 carnitine 3-dehydrogenase
The enzyme appears in viruses and cellular organisms
showSynonyms
d(+)-carnitine dehydrogenase, d-carnitine dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D(+)-carnitine dehydrogenase
-
-
-
-
D-carnitine dehydrogenase
-
-
-
-
dehydrogenase, D-carnitine
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(S)-carnitine + NAD+ = 3-dehydrocarnitine + NADH + H+
-
-
-
-
(S)-carnitine + NAD+ = 3-dehydrocarnitine + NADH + H+
specific for the (S)-enantiomer of carnitine
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
(S)-carnitine:NAD+ oxidoreductase
Specific for the (S)-enantiomer of carnitine, i.e., the enantiomer of the substrate of EC 1.1.1.108 carnitine 3-dehydrogenase
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CAS REGISTRY NUMBER
COMMENTARY
169277-49-0
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
Substrates: -
Products: -
Products: -
r
3-hydroxy-2-butanone + NAD+
2,3-butandione + NADH
-
Substrates: enzyme specific for D-carnitine
Products: -
Products: -
?
carnitine + NAD+
3-dehydrocarnitine + NADH + H+
-
Substrates: -
Products: -
Products: -
r
(S)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
Substrates: D-carnitine dehydrogenase
Products: -
Products: -
r
(S)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
Substrates: D-carnitine dehydrogenase
Products: -
Products: -
r
(S)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
Substrates: -
Products: -
Products: -
r
(S)-carnitine + NAD+
3-dehydrocarnitine + NADH + H+
-
Substrates: -
Products: -
Products: -
?
(S)-carnitine + NAD+
3-dehydrocarnitine + NADH + H+
-
Substrates: r
Products: -
Products: -
?
(S)-carnitine + NAD+
3-dehydrocarnitine + NADH + H+
-
Substrates: substrate is derived as a waste product from chemical production procedures of L(-)-carnitine
Products: formation of poly-beta-hydroxybutyrate as a storage product
Products: formation of poly-beta-hydroxybutyrate as a storage product
?
(S)-carnitine + NAD+
3-dehydrocarnitine + NADH + H+
-
Substrates: -
Products: -
Products: -
?
DL-4-amino-3-hydroxy-n-butyrate + NAD+
DL-4-amino-3-keto-n-butyrate + NADH
-
Substrates: D-carnitine dehydrogenase, less than 20% velocity compared to D-carnitine
Products: -
Products: -
?
DL-4-amino-3-hydroxy-n-butyrate + NAD+
DL-4-amino-3-keto-n-butyrate + NADH
-
Substrates: D-carnitine dehydrogenase
Products: -
Products: -
?
additional information
?
-
-
Substrates: initial step of D(+)-carnitine degradation
Products: -
Products: -
?
additional information
?
-
-
Substrates: it is expected that D-carnitine can be converted into L-carnitine by coupling reactions of D-carnitine dehydrogenase and L-carnitine dehydrogenase
Products: -
Products: -
?
additional information
?
-
-
Substrates: it is expected that D-carnitine can be converted into L-carnitine by coupling reactions of D-carnitine dehydrogenase and L-carnitine dehydrogenase
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme is induced during growth on D-carnitine
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
Substrates: -
Products: -
Products: -
r
(S)-carnitine + NAD+
3-dehydrocarnitine + NADH + H+
-
Substrates: substrate is derived as a waste product from chemical production procedures of L(-)-carnitine
Products: formation of poly-beta-hydroxybutyrate as a storage product
Products: formation of poly-beta-hydroxybutyrate as a storage product
?
(S)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
Substrates: D-carnitine dehydrogenase
Products: -
Products: -
r
(S)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
Substrates: -
Products: -
Products: -
r
additional information
?
-
-
Substrates: initial step of D(+)-carnitine degradation
Products: -
Products: -
?
additional information
?
-
-
Substrates: it is expected that D-carnitine can be converted into L-carnitine by coupling reactions of D-carnitine dehydrogenase and L-carnitine dehydrogenase
Products: -
Products: -
?
additional information
?
-
-
Substrates: it is expected that D-carnitine can be converted into L-carnitine by coupling reactions of D-carnitine dehydrogenase and L-carnitine dehydrogenase
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme is induced during growth on D-carnitine
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Mg2+
-
D-carnitine dehydrogenase, 0.5 mM, 17% increase in activity, 1.0 mM 30% increase in activity, 5.0 mM, 35% increase in activity
Ni2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoate)
-
D-carnitine dehydrogenase, 1 mM, complete inactivation
cetyltrimethylammoniumbromide
-
D-carnitine dehydrogenase, higher than 5 mM, 10% of initial activity
choline
-
D-carnitine dehydrogenase, competitive inhibition; competitive inhibitor of (S)-carnitine oxidation
crotonobetaine
-
D-carnitine dehydrogenase, competitive inhibition; competitive inhibitor of (S)-carnitine oxidation
gamma-butyrobetaine
-
D-carnitine dehydrogenase, competitive inhibition; competitive inhibitor of (S)-carnitine oxidation
glycine betaine
-
D-carnitine dehydrogenase, competitive inhibition; competitive inhibitor of (S)-carnitine oxidation
N-ethylmaleimide
-
D-carnitine dehydrogenase, 1 mM, 77% inactivation after 3 min
SDS
-
D-carnitine dehydrogenase, higher than 5 mM, 10% of initial activity; above 5 mM, 90% loss of activity
p-chloromercuribenzoate
-
D-carnitine dehydrogenase, 0.01 mM, complete inhibition
p-chloromercuribenzoate
-
D-carnitine dehydrogenase, 0.1 mM, complete inactivation
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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
14.15
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 6.5
9 - 9.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
DSM 8888, D-carnitine- and L-carnitine dehydrogenases are induced by D-carnitine and L-carnitine respectively
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
organism is able to grow on synthetic D(+)-carnitine, but not on physiological L(-)-carnitine, as sole carbon and nitrogen source
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
28000
88000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
trimer
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
40
-
D-carnitine dehydrogenase, enzyme is rapidly inactivated above 40°C
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE-Sepharose FF, TSK Butyl, Phenyl-Sepharose, Superose 12 HR, D-carnitine dehydrogenase
-
DEAE-Toyopearl, ammonium sulfate, Sephadex G-75, 5'-AMP-Sepharose 4B, Mono Q, TSK-gel G3000 SW, D-carnitine dehydrogenase
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
-
Agrobacterium radiobacter can be used for conversion of the waste product L(-)-carnitine to poly-beta-hydroxybutyrate valuable as a biodegradable and biocompatible plastic
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Setyahadi, S.; Harada, E.; Mori, N.; Kitamoto, Y.
Production of L-carnitine from D-carnitine by partially purified D- and L-carnitine dehydrogenase of Agrobacterium sp. 525a
J. Mol. Catal. , B Enzym.
4
205-209
1998
Agrobacterium sp.
-
brenda
Hanschmann, H.; Kleber, H.P.
Conversion of D-carnitine into L-carnitine with stereospecific carnitine dehydrogenase
Biotechnol. Lett.
19
679-682
1997
Agrobacterium sp.
-
brenda
Hanschmann, H.; Kleber, H.P.
Purification and characterization of D(+)-carnitine dehydrogenase from Agrobacterium sp. - a new enzyme of carnitine metabolism
Biochim. Biophys. Acta
1337
133-142
1997
Agrobacterium sp.
brenda
Obon, J.M.; Buendia, B.; Canovas, M.; Iborra, J.L.
Enzymatic cycling assay for D-carnitine determination
Anal. Biochem.
274
34-39
1999
Agrobacterium sp.
brenda
Setyahida, S.; Ueyama, T.; Arimoto, T.; Mori, N.; Kitamoto, Y.
Purification and properties of a new enzyme, D-carnitine dehydrogenase from Agrobacterium sp. 525a
Biosci. Biotechnol. Biochem.
61
1055-1058
1997
Agrobacterium sp. 525a
brenda
Kluettermann, K.; Tauchert, H.; Kleber, H.P.
Synthesis of poly-beta-hydroxybutyrate by Agrobacterium radiobacter after growth on D-carnitine
Acta Biotechnol.
22
261-269
2002
Agrobacterium tumefaciens
-
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.254)
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