BRENDA - Enzyme Database show
show all sequences of 1.1.1.108

Biochemical characterization of L-carnitine dehydrogenases from Rhizobium sp. and Xanthomonas translucens

Arima, J.; Uesumi, A.; Mitsuzumi, H.; Mori, N.; Biosci. Biotechnol. Biochem. 74, 1237-1242 (2010)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
-
Rhizobium sp.
-
Xanthomonas campestris
Engineering
Amino acid exchange
Commentary
Organism
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
Rhizobium sp.
additional information
deletion of the C-terminal 5-residue domain abolishes catalytic activity
Xanthomonas campestris
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.019
-
NAD+
mutant lacking 162 C-terminal residues, pH 8.5, 30°C
Rhizobium sp.
0.1
-
NAD+
wild-type, pH 8.5, 30°C
Rhizobium sp.
0.54
-
3-dehydrocarnitine
wild-type, pH 8.5, 30°C
Rhizobium sp.
1
-
carnitine
mutant lacking 162 C-terminal residues, pH 8.5, 30°C
Rhizobium sp.
1.2
-
3-dehydrocarnitine
mutant lacking 162 C-terminal residues, pH 8.5, 30°C
Rhizobium sp.
1.2
-
carnitine
wild-type, pH 8.5, 30°C
Rhizobium sp.
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Rhizobium sp.
D7UNT2
-
-
Xanthomonas campestris
-
-
-
Xanthomonas campestris pv. translucens
-
-
-
Posttranslational Modification
Posttranslational Modification
Commentary
Organism
additional information
enzyme has a 180-residue extra sequence at its C-terminal region with similarities to thioesterase after its first 20 amino acids
Rhizobium sp.
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.15
-
mutant lacking 168 C-terminal residues, pH 85, 30°C
Rhizobium sp.
14.5
-
mutant lacking 162 C-terminal residues, pH 85, 30°C
Rhizobium sp.
23.3
-
wild-type, pH 85, 30°C
Rhizobium sp.
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3-dehydrocarnitine + NADH + H+
-
711514
Xanthomonas campestris
carnitine + NAD+
-
-
-
?
3-dehydrocarnitine + NADH + H+
-
711514
Rhizobium sp.
carnitine + NAD+
-
-
-
?
3-dehydrocarnitine + NADH + H+
-
711514
Xanthomonas campestris pv. translucens
carnitine + NAD+
-
-
-
?
carnitine + NAD+
-
711514
Xanthomonas campestris
3-dehydrocarnitine + NADH + H+
-
-
-
r
carnitine + NAD+
-
711514
Rhizobium sp.
3-dehydrocarnitine + NADH + H+
-
-
-
r
carnitine + NAD+
-
711514
Xanthomonas campestris pv. translucens
3-dehydrocarnitine + NADH + H+
-
-
-
r
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
35
-
Tm of mutant lacking 168 C-terminal residues
Rhizobium sp.
38
-
Tm of wild-type and mutant lacking 162 C-terminal residues
Rhizobium sp.
38
-
Tm of wild-type
Xanthomonas campestris
Cloned(Commentary) (protein specific)
Commentary
Organism
-
Rhizobium sp.
-
Xanthomonas campestris
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
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
Rhizobium sp.
additional information
deletion of the C-terminal 5-residue domain abolishes catalytic activity
Xanthomonas campestris
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.019
-
NAD+
mutant lacking 162 C-terminal residues, pH 8.5, 30°C
Rhizobium sp.
0.1
-
NAD+
wild-type, pH 8.5, 30°C
Rhizobium sp.
0.54
-
3-dehydrocarnitine
wild-type, pH 8.5, 30°C
Rhizobium sp.
1
-
carnitine
mutant lacking 162 C-terminal residues, pH 8.5, 30°C
Rhizobium sp.
1.2
-
3-dehydrocarnitine
mutant lacking 162 C-terminal residues, pH 8.5, 30°C
Rhizobium sp.
1.2
-
carnitine
wild-type, pH 8.5, 30°C
Rhizobium sp.
Posttranslational Modification (protein specific)
Posttranslational Modification
Commentary
Organism
additional information
enzyme has a 180-residue extra sequence at its C-terminal region with similarities to thioesterase after its first 20 amino acids
Rhizobium sp.
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.15
-
mutant lacking 168 C-terminal residues, pH 85, 30°C
Rhizobium sp.
14.5
-
mutant lacking 162 C-terminal residues, pH 85, 30°C
Rhizobium sp.
23.3
-
wild-type, pH 85, 30°C
Rhizobium sp.
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3-dehydrocarnitine + NADH + H+
-
711514
Xanthomonas campestris
carnitine + NAD+
-
-
-
?
3-dehydrocarnitine + NADH + H+
-
711514
Rhizobium sp.
carnitine + NAD+
-
-
-
?
3-dehydrocarnitine + NADH + H+
-
711514
Xanthomonas campestris pv. translucens
carnitine + NAD+
-
-
-
?
carnitine + NAD+
-
711514
Xanthomonas campestris
3-dehydrocarnitine + NADH + H+
-
-
-
r
carnitine + NAD+
-
711514
Rhizobium sp.
3-dehydrocarnitine + NADH + H+
-
-
-
r
carnitine + NAD+
-
711514
Xanthomonas campestris pv. translucens
3-dehydrocarnitine + NADH + H+
-
-
-
r
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
35
-
Tm of mutant lacking 168 C-terminal residues
Rhizobium sp.
38
-
Tm of wild-type and mutant lacking 162 C-terminal residues
Rhizobium sp.
38
-
Tm of wild-type
Xanthomonas campestris
Other publictions for EC 1.1.1.108
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
711514
Arima
Biochemical characterization o ...
Rhizobium sp., Xanthomonas campestris, Xanthomonas campestris pv. translucens
Biosci. Biotechnol. Biochem.
74
1237-1242
2010
-
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2
-
2
-
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6
-
-
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3
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1
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3
-
6
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3
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2
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2
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6
-
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1
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-
-
3
-
6
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
700060
Wargo
Identification of genes requir ...
Pseudomonas aeruginosa
Microbiology
155
2411-2419
2009
-
-
-
-
1
-
-
-
-
-
-
-
-
5
-
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-
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-
5
-
-
-
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4
-
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-
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-
-
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-
-
-
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-
-
5
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
670345
Uanschou
-
What to learn from a comparati ...
Bacteria
Monatsh. Chem.
136
1365-1381
2005
-
1
1
-
-
-
-
-
-
-
1
1
-
1
-
-
-
-
-
1
-
-
2
1
-
-
-
-
-
-
-
1
-
-
-
-
1
1
1
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
1
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
285779
Lin
Continuous production of L-car ...
Pseudomonas putida
J. Biosci. Bioeng.
87
361-364
1999
-
1
-
-
-
-
-
-
-
-
-
2
-
2
-
-
-
-
-
-
-
-
4
-
-
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1
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1
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1
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2
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-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
285737
Hanschmann
Purification and properties of ...
Agrobacterium sp., Alcaligenes sp., Pseudomonas putida
Biochim. Biophys. Acta
1290
177-183
1996
-
-
-
-
-
-
3
8
-
-
3
3
-
4
-
-
1
-
-
-
1
-
7
1
2
-
-
-
3
-
-
3
-
-
-
-
-
-
3
-
-
-
-
3
-
8
-
-
3
3
-
-
-
1
-
-
1
-
7
1
2
-
-
-
3
-
-
-
-
-
-
-
-
-
285738
Hanschmann
-
Occurence of carnitine dehydro ...
Agrobacterium sp.
FEMS Microbiol. Lett.
119
371-376
1994
-
-
-
-
-
-
-
-
-
-
-
1
-
1
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2
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3
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1
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1
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1
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-
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2
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
285739
Mori
-
Purification and properties of ...
Rhizobium sp. YS-240
J. Ferment. Bioeng.
78
337-340
1994
-
-
-
-
-
-
11
4
-
-
2
1
-
1
-
-
1
-
-
-
1
-
2
1
1
-
1
-
2
-
1
1
-
-
-
-
-
-
1
-
-
-
-
11
-
4
-
-
2
1
-
-
-
1
-
-
1
-
2
1
1
-
1
-
2
-
1
-
-
-
-
-
-
-
285740
Matsumoto
Fluorometric determination of ...
Pseudomonas aeruginosa
Clin. Chem.
36
2072-2076
1990
-
1
-
-
-
-
-
2
-
-
-
1
-
2
-
-
-
-
-
1
1
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
1
-
-
-
-
-
-
2
-
-
-
1
-
-
-
-
-
1
1
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
285741
Goulas
Purification and properties of ...
Pseudomonas putida
Biochim. Biophys. Acta
957
335-339
1988
-
-
-
-
-
-
-
6
-
-
2
1
-
2
-
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1
-
-
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2
-
2
1
1
1
-
-
2
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
6
-
-
2
1
-
-
-
1
-
-
2
-
2
1
1
1
-
-
2
-
-
-
-
-
-
-
-
-
285742
Mori
-
Purification and some properti ...
Xanthomonas translucens
Agric. Biol. Chem.
52
249-250
1988
-
-
-
-
-
-
10
4
-
-
2
1
-
1
-
-
1
-
-
-
1
-
2
1
-
-
-
-
2
-
-
1
-
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-
1
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-
-
10
-
4
-
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2
1
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1
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1
-
2
1
-
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-
-
2
-
-
-
-
-
-
-
-
-
285743
Vandecasteele
Enzymatic synthesis of L-carni ...
Pseudomonas aeruginosa, Pseudomonas putida
Appl. Environ. Microbiol.
39
327-334
1980
-
-
-
-
-
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-
3
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2
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2
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1
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4
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2
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2
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3
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2
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1
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4
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-
285744
Schnöpp
Kinetische Untersuchungen zum ...
Pseudomonas aeruginosa
Eur. J. Biochem.
10
56-60
1969
-
-
-
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2
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1
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1
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2
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2
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1
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1
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2
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1
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2
-
2
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-
-
-
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-
-
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-
285745
Aurich
Reinigung und Eigenschaften de ...
Pseudomonas aeruginosa
Eur. J. Biochem.
6
196-201
1968
-
-
-
-
-
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5
-
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1
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1
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1
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1
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2
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1
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1
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2
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1
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1
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5
-
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1
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1
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1
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2
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1
-
1
-
2
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-
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-
-
-
285746
Aurich
An inducible carnitine dehydro ...
Pseudomonas aeruginosa
Biochim. Biophys. Acta
139
505-507
1967
-
-
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4
2
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1
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1
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2
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1
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1
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1
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4
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2
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1
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1
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