BRENDA - Enzyme Database show
show all sequences of 1.1.1.108

What to learn from a comparative genomic sequence analysis of L-carnitine dehydrogenase

Uanschou, C.; Frieht, R.; Pittner, F.; Monatsh. Chem. 136, 1365-1381 (2005)
No PubMed abstract available

Data extracted from this reference:

Application
Application
Commentary
Organism
diagnostics
the L-carnitine oxidation step can be exploited for spectroscopic L-carnitine determination in biological fluids
Bacteria
Cloned(Commentary)
Commentary
Organism
the gene encoding the enzyme is localized in a conserved genome region
Bacteria
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
35000
-
x * 35000, about, DNA sequence calculation
Bacteria
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(R)-(-)-3-hydroxy-4-(trimethylamino)butyrate + NAD+
Bacteria
i.e. L-carnitine, first step in the oxidative degradation of L-carnitine to glycine betaine
3-oxo-4-(trimethylamino)butyrate + NADH
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Bacteria
-
not in gram-positive bacteria
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
additional information
L-carnitine can serve as sole source of energy, carbon, and nitrogen
Bacteria
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(R)-(-)-3-hydroxy-4-(trimethylamino)butyrate + NAD+
i.e. L-carnitine
670345
Bacteria
3-oxo-4-(trimethylamino)butyrate + NADH
-
-
-
?
(R)-(-)-3-hydroxy-4-(trimethylamino)butyrate + NAD+
i.e. L-carnitine, first step in the oxidative degradation of L-carnitine to glycine betaine
670345
Bacteria
3-oxo-4-(trimethylamino)butyrate + NADH
-
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 35000, about, DNA sequence calculation
Bacteria
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
-
Bacteria
Application (protein specific)
Application
Commentary
Organism
diagnostics
the L-carnitine oxidation step can be exploited for spectroscopic L-carnitine determination in biological fluids
Bacteria
Cloned(Commentary) (protein specific)
Commentary
Organism
the gene encoding the enzyme is localized in a conserved genome region
Bacteria
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
-
Bacteria
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
35000
-
x * 35000, about, DNA sequence calculation
Bacteria
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(R)-(-)-3-hydroxy-4-(trimethylamino)butyrate + NAD+
Bacteria
i.e. L-carnitine, first step in the oxidative degradation of L-carnitine to glycine betaine
3-oxo-4-(trimethylamino)butyrate + NADH
-
-
?
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
additional information
L-carnitine can serve as sole source of energy, carbon, and nitrogen
Bacteria
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(R)-(-)-3-hydroxy-4-(trimethylamino)butyrate + NAD+
i.e. L-carnitine
670345
Bacteria
3-oxo-4-(trimethylamino)butyrate + NADH
-
-
-
?
(R)-(-)-3-hydroxy-4-(trimethylamino)butyrate + NAD+
i.e. L-carnitine, first step in the oxidative degradation of L-carnitine to glycine betaine
670345
Bacteria
3-oxo-4-(trimethylamino)butyrate + NADH
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 35000, about, DNA sequence calculation
Bacteria
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
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2
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6
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6
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3
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700060
Wargo
Identification of genes requir ...
Pseudomonas aeruginosa
Microbiology
155
2411-2419
2009
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1
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5
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670345
Uanschou
-
What to learn from a comparati ...
Bacteria
Monatsh. Chem.
136
1365-1381
2005
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1
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1
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285779
Lin
Continuous production of L-car ...
Pseudomonas putida
J. Biosci. Bioeng.
87
361-364
1999
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1
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2
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4
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285737
Hanschmann
Purification and properties of ...
Agrobacterium sp., Alcaligenes sp., Pseudomonas putida
Biochim. Biophys. Acta
1290
177-183
1996
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3
8
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3
3
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4
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1
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1
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7
1
2
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3
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3
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3
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1
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7
1
2
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3
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285738
Hanschmann
-
Occurence of carnitine dehydro ...
Agrobacterium sp.
FEMS Microbiol. Lett.
119
371-376
1994
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285739
Mori
-
Purification and properties of ...
Rhizobium sp. YS-240
J. Ferment. Bioeng.
78
337-340
1994
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11
4
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2
1
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2
1
1
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1
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2
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1
1
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1
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11
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4
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2
1
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2
1
1
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1
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2
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1
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285740
Matsumoto
Fluorometric determination of ...
Pseudomonas aeruginosa
Clin. Chem.
36
2072-2076
1990
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1
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2
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1
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2
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285741
Goulas
Purification and properties of ...
Pseudomonas putida
Biochim. Biophys. Acta
957
335-339
1988
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6
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2
1
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2
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6
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2
1
1
1
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2
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285742
Mori
-
Purification and some properti ...
Xanthomonas translucens
Agric. Biol. Chem.
52
249-250
1988
-
-
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10
4
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2
1
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1
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2
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1
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10
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4
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1
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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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1
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4
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285744
Schnpp
Kinetische Untersuchungen zum ...
Pseudomonas aeruginosa
Eur. J. Biochem.
10
56-60
1969
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2
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2
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2
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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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1
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5
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2
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285746
Aurich
An inducible carnitine dehydro ...
Pseudomonas aeruginosa
Biochim. Biophys. Acta
139
505-507
1967
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-
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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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4
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2
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1
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1
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