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(R)-(-)-3-hydroxy-4-(trimethylamino)butyrate + NAD+
3-oxo-4-(trimethylamino)butyrate + NADH
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
3-dehydrocarnitine + NADH + H+
carnitine + NAD+
carnitine + NAD+
3-dehydrocarnitine + NADH + H+
carnitine amide + NAD+
3-dehydrocarnitine amide + NADH + H+
-
Substrates: L-carnitine dehydrogenase, weak activity
Products: -
?
DL-4-amino-3-hydroxy-n-butyrate + NAD+
DL-4-amino-3-keto-n-butyrate + NADH
-
Substrates: -
Products: -
?
(R)-(-)-3-hydroxy-4-(trimethylamino)butyrate + NAD+
3-oxo-4-(trimethylamino)butyrate + NADH
-
Substrates: i.e. L-carnitine
Products: -
?
(R)-(-)-3-hydroxy-4-(trimethylamino)butyrate + NAD+
3-oxo-4-(trimethylamino)butyrate + NADH
-
Substrates: i.e. L-carnitine, first step in the oxidative degradation of L-carnitine to glycine betaine
Products: -
?
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
Substrates: -
Products: -
r
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
Substrates: -
Products: -
r
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
Substrates: -
Products: -
r
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
Substrates: -
Products: -
r
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
Substrates: -
Products: -
r
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
Substrates: -
Products: -
r
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
Substrates: -
Products: -
r
3-dehydrocarnitine + NADH + H+
carnitine + NAD+
Substrates: -
Products: -
?
3-dehydrocarnitine + NADH + H+
carnitine + NAD+
-
Substrates: -
Products: -
?
3-dehydrocarnitine + NADH + H+
carnitine + NAD+
-
Substrates: -
Products: -
?
carnitine + NAD+
3-dehydrocarnitine + NADH + H+
-
Substrates: -
Products: -
r
carnitine + NAD+
3-dehydrocarnitine + NADH + H+
-
Substrates: -
Products: -
r
carnitine + NAD+
3-dehydrocarnitine + NADH + H+
-
Substrates: -
Products: -
r
carnitine + NAD+
3-dehydrocarnitine + NADH + H+
Substrates: 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
Products: -
?
carnitine + NAD+
3-dehydrocarnitine + NADH + H+
Substrates: 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
Products: -
?
carnitine + NAD+
3-dehydrocarnitine + NADH + H+
-
Substrates: -
Products: -
r
carnitine + NAD+
3-dehydrocarnitine + NADH + H+
-
Substrates: -
Products: -
r
carnitine + NAD+
3-dehydrocarnitine + NADH + H+
-
Substrates: -
Products: -
r
carnitine + NAD+
3-dehydrocarnitine + NADH + H+
Substrates: -
Products: -
r
carnitine + NAD+
3-dehydrocarnitine + NADH + H+
-
Substrates: -
Products: -
r
carnitine + NAD+
3-dehydrocarnitine + NADH + H+
-
Substrates: -
Products: -
r
carnitine + NAD+
3-dehydrocarnitine + NADH + H+
-
Substrates: -
Products: -
r
carnitine + NAD+
3-dehydrocarnitine + NADH + H+
-
Substrates: -
Products: -
?
carnitine + NAD+
3-dehydrocarnitine + NADH + H+
-
Substrates: -
Products: -
r
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(R)-(-)-3-hydroxy-4-(trimethylamino)butyrate + NAD+
3-oxo-4-(trimethylamino)butyrate + NADH
-
Substrates: i.e. L-carnitine, first step in the oxidative degradation of L-carnitine to glycine betaine
Products: -
?
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
carnitine + NAD+
3-dehydrocarnitine + NADH + H+
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
Substrates: -
Products: -
r
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
Substrates: -
Products: -
r
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
Substrates: -
Products: -
r
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
Substrates: -
Products: -
r
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
Substrates: -
Products: -
r
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
Substrates: -
Products: -
r
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
3-dehydrocarnitine + NADH + H+
-
Substrates: -
Products: -
r
carnitine + NAD+
3-dehydrocarnitine + NADH + H+
-
Substrates: -
Products: -
r
carnitine + NAD+
3-dehydrocarnitine + NADH + H+
-
Substrates: -
Products: -
?
carnitine + NAD+
3-dehydrocarnitine + NADH + H+
-
Substrates: -
Products: -
r
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0.54 - 1.71
3-dehydrocarnitine
0.54
3-dehydrocarnitine
-
-
0.54
3-dehydrocarnitine
wild-type, pH 8.5, 30°C
0.72
3-dehydrocarnitine
-
L-carnitine dehydrogenase
1.1
3-dehydrocarnitine
-
potassium phosphate buffer, pH 7
1.2
3-dehydrocarnitine
mutant lacking 162 C-terminal residues, pH 8.5, 30°C
1.25
3-dehydrocarnitine
-
-
1.3
3-dehydrocarnitine
-
-
1.54
3-dehydrocarnitine
-
Tris-HCl buffer, pH 9
1.71
3-dehydrocarnitine
-
-
1
carnitine
mutant lacking 162 C-terminal residues, pH 8.5, 30°C
1.07
carnitine
-
wild type enzyme, at pH 9.5 and 30°C
1.2
carnitine
wild-type, pH 8.5, 30°C
1.21
carnitine
-
mutant enzyme S220G/F221A, at pH 9.5 and 30°C
1.61
carnitine
-
mutant enzyme Y140F, at pH 9.5 and 30°C
1.72
carnitine
-
mutant enzyme A185G, at pH 9.5 and 30°C
10.2
carnitine
-
wild type enzyme, at pH 9.5, temperature not specified in the publication
10.38
carnitine
-
wild type enzyme, at pH 9.5 and 30°C
18.66
carnitine
-
mutant enzyme Y140W, at pH 9.5 and 30°C
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
96.2
carnitine
-
mutant enzyme G223S/A224F, at pH 9.5 and 30°C
96.2
carnitine
-
mutant enzyme I190V/A191G, at pH 9.5 and 30°C
101.4
carnitine
-
mutant enzyme Q252A, at pH 9.5, temperature not specified in the publication
137
carnitine
-
mutant enzyme F143Y, at pH 9.5 and 30°C
137
carnitine
-
mutant enzyme G188A, at pH 9.5 and 30°C
144.9
carnitine
-
mutant enzyme F143C, at pH 9.5 and 30°C
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
240.3
carnitine
-
mutant enzyme F143H, at pH 9.5 and 30°C
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
313.6
carnitine
-
mutant enzyme Y140C, at pH 9.5 and 30°C
321.5
carnitine
-
mutant enzyme F143K, at pH 9.5 and 30°C
330.1
carnitine
-
mutant enzyme Y140S, at pH 9.5 and 30°C
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
353.8
carnitine
-
mutant enzyme F143A, at pH 9.5 and 30°C
477.8
carnitine
-
mutant enzyme F143N, at pH 9.5 and 30°C
667
carnitine
-
mutant enzyme S120A, at pH 9.5, temperature not specified in the publication
723.4
carnitine
-
mutant enzyme F143S, at pH 9.5 and 30°C
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
2955
carnitine
-
mutant enzyme F143G, at pH 9.5 and 30°C
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
8.9
L-carnitine
-
at pH 9.0
26
L-carnitine
-
at pH 9.5
0.018
NAD+
-
L-carnitine dehydrogenase, two different forms of the enzyme or two binding sites
0.019
NAD+
mutant lacking 162 C-terminal residues, pH 8.5, 30°C
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
0.09
NAD+
-
wild type enzyme, at pH 9.5 and 30°C
0.1
NAD+
wild-type, pH 8.5, 30°C
0.11
NAD+
-
mutant enzyme S220G/F221A, at pH 9.5 and 30°C
0.13
NAD+
-
mutant enzyme Y140F, at pH 9.5 and 30°C
0.15
NAD+
-
mutant enzyme A185G, at pH 9.5 and 30°C
0.21
NAD+
-
mutant enzyme Y140S, at pH 9.5 and 30°C
0.24
NAD+
-
mutant enzyme G223S/A224F, at pH 9.5 and 30°C
0.24
NAD+
-
mutant enzyme I190V/A191G, at pH 9.5 and 30°C
0.24
NAD+
-
mutant enzyme Y140W, at pH 9.5 and 30°C
0.25
NAD+
-
mutant enzyme Y140C, at pH 9.5 and 30°C
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
0.32
NAD+
-
mutant enzyme F143Y, at pH 9.5 and 30°C
0.32
NAD+
-
wild type enzyme, at pH 9.5 and 30°C
0.33
NAD+
-
mutant enzyme F143C, at pH 9.5 and 30°C
0.33
NAD+
-
mutant enzyme F143H, at pH 9.5 and 30°C
0.34
NAD+
-
mutant enzyme F143N, at pH 9.5 and 30°C
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
0.36
NAD+
-
mutant enzyme F143A, at pH 9.5 and 30°C
0.37
NAD+
-
mutant enzyme F143G, at pH 9.5 and 30°C
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
0.42
NAD+
-
mutant enzyme F143S, at pH 9.5 and 30°C
0.44
NAD+
-
mutant enzyme G188A, at pH 9.5 and 30°C
0.53
NAD+
-
mutant enzyme T262A, at pH 9.5, temperature not specified in the publication
0.88
NAD+
-
mutant enzyme F143K, at pH 9.5 and 30°C
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
0.013
NADH
-
potassium phosphate buffer, pH 7
0.032
NADH
-
L-carnitine dehydrogenase
0.067
NADH
-
Tris-HCl buffer, pH 9
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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
0.002
carnitine
-
mutant enzyme F143G, at pH 9.5 and 30°C
0.003
carnitine
-
mutant enzyme Y140S, at pH 9.5 and 30°C
0.003
carnitine
-
mutant enzyme Y147A, at pH 9.5, temperature not specified in the publication
0.006
carnitine
-
mutant enzyme F143S, at pH 9.5 and 30°C
0.007
carnitine
-
mutant enzyme F143A, at pH 9.5 and 30°C
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
0.01
carnitine
-
mutant enzyme Y140C, at pH 9.5 and 30°C
0.013
carnitine
-
mutant enzyme Y237A, at pH 9.5, temperature not specified in the publication
0.016
carnitine
-
mutant enzyme F143K, at pH 9.5 and 30°C
0.016
carnitine
-
mutant enzyme R297A, at pH 9.5, temperature not specified in the publication
0.017
carnitine
-
mutant enzyme F143N, at pH 9.5 and 30°C
0.019
carnitine
-
mutant enzyme S117A, at pH 9.5, temperature not specified in the publication
0.039
carnitine
-
mutant enzyme F143H, at pH 9.5 and 30°C
0.044
carnitine
-
mutant enzyme M246A, at pH 9.5, temperature not specified in the publication
0.05
carnitine
-
mutant enzyme F143Y, at pH 9.5 and 30°C
0.051
carnitine
-
mutant enzyme F143C, at pH 9.5 and 30°C
0.068
carnitine
-
mutant enzyme T262A, at pH 9.5, temperature not specified in the publication
0.079
carnitine
-
mutant enzyme N144A, at pH 9.5, temperature not specified in the publication
0.157
carnitine
-
mutant enzyme Q252A, at pH 9.5, temperature not specified in the publication
0.22
carnitine
-
mutant enzyme E185A, at pH 9.5, temperature not specified in the publication
0.236
carnitine
-
mutant enzyme Y140W, at pH 9.5 and 30°C
0.37
carnitine
-
mutant enzyme G233S/A224F, at pH 9.5 and 30°C
0.37
carnitine
-
mutant enzyme I190V/A191G, at pH 9.5 and 30°C
1.19
carnitine
-
mutant enzyme G188A, at pH 9.5 and 30°C
1.279
carnitine
-
wild type enzyme, at pH 9.5, temperature not specified in the publication
1.97
carnitine
-
wild type enzyme, at pH 9.5 and 30°C
6.03
carnitine
-
mutant enzyme A185G, at pH 9.5 and 30°C
9.796
carnitine
-
mutant enzyme Y140F, at pH 9.5 and 30°C
11.36
carnitine
-
mutant enzyme S220G/F221A, at pH 9.5 and 30°C
11.77
carnitine
-
wild type enzyme, at pH 9.5 and 30°C
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A185G
-
the mutant shows reduced activity compared to the wild type enzyme
S220G/F221A
-
the mutant shows reduced activity compared to the wild type enzyme
Y140C
-
the mutant shows reduced activity compared to the wild type enzyme
Y140F
-
the mutant shows reduced activity compared to the wild type enzyme
Y140S
-
the mutant shows reduced activity compared to the wild type enzyme
Y140W
-
the mutant shows reduced activity compared to the wild type enzyme
E185A
-
the mutant shows reduced activity compared to the wild type enzyme
E201A
-
the mutant shows reduced activity compared to the wild type enzyme
F143A
-
the mutant shows reduced activity compared to the wild type enzyme
F143C
-
the mutant shows reduced activity compared to the wild type enzyme
F143G
-
the mutant shows reduced activity compared to the wild type enzyme
F143H
-
the mutant shows reduced activity compared to the wild type enzyme
F143K
-
the mutant shows reduced activity compared to the wild type enzyme
F143N
-
the mutant shows reduced activity compared to the wild type enzyme
F143S
-
the mutant shows reduced activity compared to the wild type enzyme
F143Y
-
the mutant shows reduced activity compared to the wild type enzyme
F189A
-
the mutant shows reduced activity compared to the wild type enzyme
F234A
-
the mutant shows reduced activity compared to the wild type enzyme
G188A
-
the mutant shows reduced activity compared to the wild type enzyme
G233S/A224F
-
the mutant shows reduced activity compared to the wild type enzyme
I190V/A191G
-
the mutant shows reduced activity compared to the wild type enzyme
M231A
-
the mutant shows reduced activity compared to the wild type enzyme
M246A
-
the mutant shows reduced activity compared to the wild type enzyme
N144A
-
the mutant shows reduced activity compared to the wild type enzyme
Q252A
-
the mutant shows reduced activity compared to the wild type enzyme
R200A
-
the mutant shows reduced activity compared to the wild type enzyme
R297A
-
the mutant shows reduced activity compared to the wild type enzyme
S117A
-
the mutant shows reduced activity compared to the wild type enzyme
S120A
-
the mutant shows reduced activity compared to the wild type enzyme
T262A
-
the mutant shows reduced activity compared to the wild type enzyme
W228A
-
the mutant shows reduced activity compared to the wild type enzyme
Y147A
-
the mutant shows reduced activity compared to the wild type enzyme
Y237A
-
the mutant shows reduced activity compared to the wild type enzyme
additional information
-
strain PA14 mutants with transposon insertions in PA5385 and PA5388 result in the inability of Pseudomonas aeruginosa to grow on carnitine, mutants from the PAO1 transposon insertions in each of the PA5388, PA5387, PA5386 and PA5388 genes are unable to grow on carnitine
additional information
strain PA14 mutants with transposon insertions in PA5385 and PA5388 result in the inability of Pseudomonas aeruginosa to grow on carnitine, mutants from the PAO1 transposon insertions in each of the PA5388, PA5387, PA5386 and PA5388 genes are unable to grow on carnitine
additional information
deletion of the C-terminal thioesterase domain, mutant DELTA162-CDH, only slightly affects enzymic activity. Activity is eliminated by deletion of the whole C-terminal extra sequence in mutants DELTA168-CDH, DELTA174-CDH, DELTA178-CDH
additional information
-
deletion of the C-terminal 5-residue domain abolishes catalytic activity
additional information
-
deletion of the C-terminal 5-residue domain abolishes catalytic activity
-
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Hanschmann, H.; Ehricht, R.; Kleber, H.P.
Purification and properties of L(-)-carnitine dehydrogenase from Agrobacterium sp.
Biochim. Biophys. Acta
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177-183
1996
Agrobacterium sp., Alcaligenes sp., Pseudomonas putida
brenda
Hanschmann, H.; Doss, A.; Kleber, H.P.
Occurence of carnitine dehydrogenases with different stereospecificity in agrobacterium sp.
FEMS Microbiol. Lett.
119
371-376
1994
Agrobacterium sp.
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brenda
Mori, N.; Mitsuzumi, H.; Kitamoto, Y.
Purification and properties of carnitine dehydrogenase from Pseudomonas sp. YS-240
J. Ferment. Bioeng.
78
337-340
1994
Rhizobium sp. YS-240
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brenda
Matsumoto, K.; Yamada, Y.; Takahasi, M.; Todoroki, T.; Mizoguchi, K.; Misaki, H.; Yuki, H.
Fluorometric determination of carnitine in serum with immobilized carnitine dehydrogenase and diaphorase
Clin. Chem.
36
2072-2076
1990
Pseudomonas aeruginosa
brenda
Goulas, P.
Purification and properties of carnitine dehydrogenase from Pseudomonas putida
Biochim. Biophys. Acta
957
335-339
1988
Pseudomonas putida
brenda
Mori, N.; Kasugai, T.; Kitamoto, Y.; Ichikawa, Y.
Purification and some properties of carnitine dehydrogenase from Xanthomonas translucens
Agric. Biol. Chem.
52
249-250
1988
Xanthomonas translucens
-
brenda
Vandecasteele, J-P.
Enzymatic synthesis of L-carnitine by reduction of an achiral precursor: the problem of reduced nicotinamide adenine dinucleotide recycling
Appl. Environ. Microbiol.
39
327-334
1980
Pseudomonas aeruginosa, Pseudomonas putida
brenda
Schnpp, W.; Sorger, H.; Kleber, H-P.; Aurich, H.
Kinetische Untersuchungen zum Reaktionsmechanismus der Carnitindehydrogenase aus Pseudomonas aeruginosa
Eur. J. Biochem.
10
56-60
1969
Pseudomonas aeruginosa
brenda
Aurich, H.; Kleber, H.P.; Sorger, H.; Tauchert, H.
Reinigung und Eigenschaften der Carnitindehydrogenase
Eur. J. Biochem.
6
196-201
1968
Pseudomonas aeruginosa
brenda
Aurich, H.; Kleber, H.P.; Schpp, W.D.
An inducible carnitine dehydrogenase from Pseudomonas aeruginosa
Biochim. Biophys. Acta
139
505-507
1967
Pseudomonas aeruginosa
brenda
Lin, S.S.; Miyawaki, O.; Nakamura, K.
Continuous production of L-carnitine with NADH regeneration by a nanofiltration membrane reactor with coimmobilized L-carnitine dehydrogenase and glucose dehydrogenase
J. Biosci. Bioeng.
87
361-364
1999
Pseudomonas putida
brenda
Uanschou, C.; Frieht, R.; Pittner, F.
What to learn from a comparative genomic sequence analysis of L-carnitine dehydrogenase
Monatsh. Chem.
136
1365-1381
2005
Bacteria
-
brenda
Wargo, M.J.; Hogan, D.A.
Identification of genes required for Pseudomonas aeruginosa carnitine catabolism
Microbiology
155
2411-2419
2009
Pseudomonas aeruginosa, Pseudomonas aeruginosa (Q9HTH8)
brenda
Arima, J.; Uesumi, A.; Mitsuzumi, H.; Mori, N.
Biochemical characterization of L-carnitine dehydrogenases from Rhizobium sp. and Xanthomonas translucens
Biosci. Biotechnol. Biochem.
74
1237-1242
2010
Rhizobium sp. (D7UNT2), Xanthomonas campestris, Xanthomonas campestris pv. translucens
brenda
Eltayeb, M.M.; Arima, J.; Mori, N.
Alanine-scanning mutation approach for classification of the roles of conserved residues in the activity and substrate affinity of L-carnitine dehydrogenase
Biotechnol. Lett.
36
309-317
2014
Xanthomonas translucens
brenda
Eltayeb, M.M.; Mohamed Ahmed, I.A.; Arima, J.; Mori, N.
Identification of residues essential for the activity and substrate affinity of L-carnitine dehydrogenase
Mol. Biotechnol.
55
268-276
2013
Rhizobium sp., Xanthomonas translucens
brenda