Information on EC 1.1.1.108 - carnitine 3-dehydrogenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.1.108
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RECOMMENDED NAME
GeneOntology No.
carnitine 3-dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
carnitine + NAD+ = 3-dehydrocarnitine + NADH + H+
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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-
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reduction
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
carnitine metabolism
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L-carnitine degradation II
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D-carnitine degradation II
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SYSTEMATIC NAME
IUBMB Comments
carnitine:NAD+ 3-oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY hide
9045-45-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
not in gram-positive bacteria
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-(-)-3-hydroxy-4-(trimethylamino)butyrate + NAD+
3-oxo-4-(trimethylamino)butyrate + NADH
show the reaction diagram
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
show the reaction diagram
3-dehydrocarnitine + NADH + H+
carnitine + NAD+
show the reaction diagram
carnitine + NAD+
3-dehydrocarnitine + NADH + H+
show the reaction diagram
carnitine amide + NAD+
3-dehydrocarnitine amide + NADH + H+
show the reaction diagram
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L-carnitine dehydrogenase, weak activity
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?
DL-4-amino-3-hydroxy-n-butyrate + NAD+
DL-4-amino-3-keto-n-butyrate + NADH
show the reaction diagram
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(R)-(-)-3-hydroxy-4-(trimethylamino)butyrate + NAD+
3-oxo-4-(trimethylamino)butyrate + NADH
show the reaction diagram
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i.e. L-carnitine, first step in the oxidative degradation of L-carnitine to glycine betaine
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-
?
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
show the reaction diagram
carnitine + NAD+
3-dehydrocarnitine + NADH + H+
show the reaction diagram
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-deydrocarnitine
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competitive inhibition vs. L-carnitine
5,5'-dithiobis(2-nitrobenzoate)
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Cu+
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60-70% inhibition
Hydrazine hydrate
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30 mM, 70% inhibition
hydroxylamine
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1 mM, complete inhibition
NADH
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competitive inhibition vs. NAD+
Ni2+
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strong inhibition
o-phenanthroline
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38% inhibition
p-chloromercuribenzoate
Sodium borate
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20 mM, 60% inhibition
trimethylamine
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L-carnitine dehydrogenase, strong inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.54 - 1.71
3-dehydrocarnitine
1 - 2955
carnitine
0.29 - 26
L-carnitine
0.018 - 9.66
NAD+
0.013 - 0.067
NADH
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.001 - 11.77
carnitine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.13
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D-carnitine dehydrogenase, after DEAE-Sepharose FF chromatography of cell extracts
0.15
mutant lacking 168 C-terminal residues, pH 85, 30°C
0.35
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L-carnitine dehydrogenase, after DEAE-Sepharose FF chromatography of cell extracts
1.2
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L-carnitine dehydrogenase activity in crude extracts
14.5
mutant lacking 162 C-terminal residues, pH 85, 30°C
16.75
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L-carnitine dehydrogenase
200
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oxidation of L-carnitine
240
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reduction of 3-dehydrocarnitine at pH 7-7.5
600
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reduction of 3-dehydrocarnitine
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.6 - 6.5
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L-carnitine dehydrogenase, oxidation of L-carnitine
6.5 - 8
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reduction of 3-dehydrocarnitine
6.5
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reduction of 3-dehydrocarnitine
7
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reduction of 3-dehydrocarnitine
7 - 7.5
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reduction of 3-dehydrocarnitine
9
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oxidation of L-carnitine
9 - 9.5
9
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oxidation of L-carnitine
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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activity declines rapidly above 35°C
45
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L-carnitine dehydrogenase
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
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L-carnitine can serve as sole source of energy, carbon, and nitrogen
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32000
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2 * 32000, SDS-PAGE
35000
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x * 35000, about, DNA sequence calculation
37000
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2 * 37000, SDS-PAGE
50000
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2 * 50000, SDS-PAGE
51000
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gel filtration
57000
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2 * 57000, L-carnitine dehydrogenase, SDS-PAGE
60000
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gel filtration
74000
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gel filtration
110000
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gel filtration
114000
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gel filtration, L-carnitine dehydrogenase
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
enzyme has a 180-residue extra sequence at its C-terminal region with similarities to thioesterase after its first 20 amino acids
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8
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285739
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
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the enzyme retains about 29% of its initial activity after incubation for 30 min at 40°C
45
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the enzyme retains 100% activity after incubation for 30 min at 45°C
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, DEAE-cellulose, Sephadex G-100, 5'-AMP Sepharose 4B, Sephadex G-100
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ammonium sulfate, Sephadex G-200, 5'-AMP-Sepharose 4B, gel filtration
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ammonium sulfate, Sephadex G-200, hydroxylapatite
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amylose resin column chromatography
amylose resin column chromatography, and Superdex 200 gel filtration
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DEAE-Sepharose FF, Blue-Sepharose, Superose 12HR, Fractogel TSK Butyl, L-carnitine dehydrogenase
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DEAE-Toyopearl, ammonium sulfate, hydroxylapatite, Sephacryl S-200, hydroxylapatite
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli JM109 cells
the gene encoding the enzyme is localized in a conserved genome region
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A185G
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the mutant shows reduced activity compared to the wild type enzyme
S220G/F221A
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the mutant shows reduced activity compared to the wild type enzyme
V187I/G188A
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inactive
Y140A
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inactive
Y140C
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the mutant shows reduced activity compared to the wild type enzyme
Y140D
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inactive
Y140F
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the mutant shows reduced activity compared to the wild type enzyme
Y140G
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inactive
Y140H
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inactive
Y140K
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inactive
Y140N
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inactive
Y140S
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the mutant shows reduced activity compared to the wild type enzyme
Y140W
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the mutant shows reduced activity compared to the wild type enzyme
D298A
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inactive
E185A
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the mutant shows reduced activity compared to the wild type enzyme
E196A
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inactive
E201A
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the mutant shows reduced activity compared to the wild type enzyme
F143A
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the mutant shows reduced activity compared to the wild type enzyme
F143C
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the mutant shows reduced activity compared to the wild type enzyme
F143D
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inactive
F143G
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the mutant shows reduced activity compared to the wild type enzyme
F143H
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the mutant shows reduced activity compared to the wild type enzyme
F143K
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the mutant shows reduced activity compared to the wild type enzyme
F143N
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the mutant shows reduced activity compared to the wild type enzyme
F143S
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the mutant shows reduced activity compared to the wild type enzyme
F143W
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inactive
F143Y
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the mutant shows reduced activity compared to the wild type enzyme
F189A
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the mutant shows reduced activity compared to the wild type enzyme
F234A
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the mutant shows reduced activity compared to the wild type enzyme
F249A
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inactive
F253A
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inactive
G188A
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the mutant shows reduced activity compared to the wild type enzyme
G233S/A224F
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the mutant shows reduced activity compared to the wild type enzyme
I190V/A191G
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the mutant shows reduced activity compared to the wild type enzyme
M231A
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the mutant shows reduced activity compared to the wild type enzyme
M246A
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the mutant shows reduced activity compared to the wild type enzyme
N144A
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the mutant shows reduced activity compared to the wild type enzyme
Q252A
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the mutant shows reduced activity compared to the wild type enzyme
R193A
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inactive
R200A
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the mutant shows reduced activity compared to the wild type enzyme
R297A
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the mutant shows reduced activity compared to the wild type enzyme
S117A
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the mutant shows reduced activity compared to the wild type enzyme
S120A
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the mutant shows reduced activity compared to the wild type enzyme
T262A
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the mutant shows reduced activity compared to the wild type enzyme
W199A
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inactive
W228A
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the mutant shows reduced activity compared to the wild type enzyme
W261A
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inactive
Y147A
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the mutant shows reduced activity compared to the wild type enzyme
Y237A
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the mutant shows reduced activity compared to the wild type enzyme
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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fluorometric determination of carnitine in serum with immobilized carnitine dehydrogenase and diaphorase
diagnostics
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the L-carnitine oxidation step can be exploited for spectroscopic L-carnitine determination in biological fluids
synthesis
Show AA Sequence (1392 entries)
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