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Information on EC 1.1.1.108 - carnitine 3-dehydrogenase
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1.1.1.108 carnitine 3-dehydrogenaseSpecify your search results
Word Map
- 1.1.1.108
-
hernia
-
diaphragmatic
-
prenatal
-
fetuses
-
survivors
- anomalies
-
extracorporeal
-
neurodevelopmental
-
multicenter
-
xanthomonas
-
circumference
-
herniation
-
antenatal
- translucens
- trimethylamine
-
single-institution
-
alanine-scanning
-
between-run
- synthesis
- analysis
- diagnostics
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
l-cdh, l-carnitine dehydrogenase, l-(-)-carnitine dehydrogenase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Cdh
L-carnitine dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
carnitine + NAD+ = 3-dehydrocarnitine + NADH + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
carnitine:NAD+ 3-oxidoreductase
-
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CAS REGISTRY NUMBER
COMMENTARY
9045-45-8
-
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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
(R)-(-)-3-hydroxy-4-(trimethylamino)butyrate + NAD+
3-oxo-4-(trimethylamino)butyrate + NADH
carnitine amide + NAD+
3-dehydrocarnitine amide + NADH + H+
-
L-carnitine dehydrogenase, weak activity
-
?
DL-4-amino-3-hydroxy-n-butyrate + NAD+
DL-4-amino-3-keto-n-butyrate + NADH
-
-
-
?
(R)-(-)-3-hydroxy-4-(trimethylamino)butyrate + NAD+
3-oxo-4-(trimethylamino)butyrate + NADH
-
i.e. L-carnitine
-
-
?
(R)-(-)-3-hydroxy-4-(trimethylamino)butyrate + NAD+
3-oxo-4-(trimethylamino)butyrate + NADH
-
i.e. L-carnitine, first step in the oxidative degradation of L-carnitine to glycine betaine
-
-
?
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
-
-
r
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
-
-
r
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
-
-
r
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
-
-
r
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
-
-
r
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
-
-
r
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
-
-
r
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
-
-
r
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
-
-
r
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
-
-
r
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
-
-
r
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
-
-
r
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
-
-
r
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
-
-
r
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
-
-
r
3-dehydrocarnitine + NADH + H+
carnitine + NAD+
-
-
-
-
?
carnitine + NAD+
3-dehydrocarnitine + NADH + H+
the PA5388-PA5384 region contains the predicted carnitine dehydrogenase homologue along with other genes required for growth on carnitine. The PA5389 transcription factor (CDHR) is required for growth on carnitine, it is required for induction of the PA5388-PA5384 transcripts in response to carnitine
-
-
?
carnitine + NAD+
3-dehydrocarnitine + NADH + H+
the PA5389 transcription factor (CDHR) is required for growth on carnitine, it is required for induction of the PA5388-PA5384 transcripts in response to carnitine
-
-
?
carnitine + NAD+
3-dehydrocarnitine + NADH + H+
-
-
-
-
r
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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
(R)-(-)-3-hydroxy-4-(trimethylamino)butyrate + NAD+
3-oxo-4-(trimethylamino)butyrate + NADH
-
i.e. L-carnitine, first step in the oxidative degradation of L-carnitine to glycine betaine
-
-
?
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
-
-
r
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
-
-
r
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
-
-
r
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
-
-
r
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
-
-
r
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
-
-
r
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
-
-
r
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
-
-
r
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
-
-
r
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
-
-
r
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
-
-
r
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
-
-
r
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
-
-
r
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
-
-
r
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
-
-
r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Congenital Abnormalities
Population-based analysis of left- and right-sided diaphragmatic hernias demonstrates different frequencies of selected additional anomalies.
Gastroesophageal Reflux
Outcome of right-sided diaphragmatic hernia repair: a multicentre study.
Heart Septal Defects, Atrial
Population-based analysis of left- and right-sided diaphragmatic hernias demonstrates different frequencies of selected additional anomalies.
Polydactyly
Population-based analysis of left- and right-sided diaphragmatic hernias demonstrates different frequencies of selected additional anomalies.
Syndactyly
Population-based analysis of left- and right-sided diaphragmatic hernias demonstrates different frequencies of selected additional anomalies.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.2
3-dehydrocarnitine
mutant lacking 162 C-terminal residues, pH 8.5, 30°C
10.2
carnitine
-
wild type enzyme, at pH 9.5, temperature not specified in the publication
40.4
carnitine
-
mutant enzyme E185A, at pH 9.5, temperature not specified in the publication
89.1
carnitine
-
mutant enzyme T262A, at pH 9.5, temperature not specified in the publication
101.4
carnitine
-
mutant enzyme Q252A, at pH 9.5, temperature not specified in the publication
164
carnitine
-
mutant enzyme N144A, at pH 9.5, temperature not specified in the publication
205.7
carnitine
-
mutant enzyme F189A, at pH 9.5, temperature not specified in the publication
284
carnitine
-
mutant enzyme Y147A, at pH 9.5, temperature not specified in the publication
307.6
carnitine
-
mutant enzyme S117A, at pH 9.5, temperature not specified in the publication
308.8
carnitine
-
mutant enzyme M231A, at pH 9.5, temperature not specified in the publication
331.9
carnitine
-
mutant enzyme Y147A, at pH 9.5, temperature not specified in the publication
336.2
carnitine
-
mutant enzyme M246A, at pH 9.5, temperature not specified in the publication
667
carnitine
-
mutant enzyme S120A, at pH 9.5, temperature not specified in the publication
767.1
carnitine
-
mutant enzyme R200A, at pH 9.5, temperature not specified in the publication
799.7
carnitine
-
mutant enzyme Y237A, at pH 9.5, temperature not specified in the publication
830.7
carnitine
-
mutant enzyme R297A, at pH 9.5, temperature not specified in the publication
1010
carnitine
-
mutant enzyme W228A, at pH 9.5, temperature not specified in the publication
1056
carnitine
-
mutant enzyme F234A, at pH 9.5, temperature not specified in the publication
2000
carnitine
-
Km above 2000 mM, mutant enzyme D298A, at pH 9.5, temperature not specified in the publication
2000
carnitine
-
Km above 2000 mM, mutant enzyme F249A, at pH 9.5, temperature not specified in the publication
2000
carnitine
-
Km above 2000 mM, mutant enzyme F253A, at pH 9.5, temperature not specified in the publication
2000
carnitine
-
Km above 2000 mM, mutant enzyme W261A, at pH 9.5, temperature not specified in the publication
0.29
L-carnitine
-
L-carnitine dehydrogenase, two different forms of the enzyme or two binding sites
6.1
L-carnitine
-
L-carnitine dehydrogenase, two different forms of the enzyme or two binding sites
0.018
NAD+
-
L-carnitine dehydrogenase, two different forms of the enzyme or two binding sites
0.042
NAD+
-
L-carnitine dehydrogenase, two different forms of the enzyme or two binding sites
0.07
NAD+
-
mutant enzyme W228A, at pH 9.5, temperature not specified in the publication
0.08
NAD+
-
mutant enzyme Y147A, at pH 9.5, temperature not specified in the publication
0.09
NAD+
-
mutant enzyme F234A, at pH 9.5, temperature not specified in the publication
0.09
NAD+
-
mutant enzyme M231A, at pH 9.5, temperature not specified in the publication
0.26
NAD+
-
mutant enzyme R297A, at pH 9.5, temperature not specified in the publication
0.31
NAD+
-
wild type enzyme, at pH 9.5, temperature not specified in the publication
0.35
NAD+
-
mutant enzyme N144A, at pH 9.5, temperature not specified in the publication
0.35
NAD+
-
mutant enzyme Y147A, at pH 9.5, temperature not specified in the publication
0.36
NAD+
-
mutant enzyme E185A, at pH 9.5, temperature not specified in the publication
0.39
NAD+
-
mutant enzyme M246A, at pH 9.5, temperature not specified in the publication
0.39
NAD+
-
mutant enzyme Y237A, at pH 9.5, temperature not specified in the publication
0.4
NAD+
-
mutant enzyme Q252A, at pH 9.5, temperature not specified in the publication
0.53
NAD+
-
mutant enzyme T262A, at pH 9.5, temperature not specified in the publication
1.04
NAD+
-
mutant enzyme F189A, at pH 9.5, temperature not specified in the publication
2.25
NAD+
-
mutant enzyme R200A, at pH 9.5, temperature not specified in the publication
3.76
NAD+
-
mutant enzyme S117A, at pH 9.5, temperature not specified in the publication
9.66
NAD+
-
mutant enzyme S120A, at pH 9.5, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.001
carnitine
-
mutant enzyme F234A, at pH 9.5, temperature not specified in the publication
0.001
carnitine
-
mutant enzyme R200A, at pH 9.5, temperature not specified in the publication
0.001
carnitine
-
mutant enzyme S120A, at pH 9.5, temperature not specified in the publication
0.003
carnitine
-
mutant enzyme Y147A, at pH 9.5, temperature not specified in the publication
0.007
carnitine
-
mutant enzyme Y147A, at pH 9.5, temperature not specified in the publication
0.008
carnitine
-
mutant enzyme W228A, at pH 9.5, temperature not specified in the publication
0.009
carnitine
-
mutant enzyme F189A, at pH 9.5, temperature not specified in the publication
0.01
carnitine
-
mutant enzyme M231A, at pH 9.5, temperature not specified in the publication
0.013
carnitine
-
mutant enzyme Y237A, at pH 9.5, temperature not specified in the publication
0.016
carnitine
-
mutant enzyme R297A, at pH 9.5, temperature not specified in the publication