BRENDA - Enzyme Database show
show all sequences of 1.1.1.254

Purification and characterization of D(+)-carnitine dehydrogenase from Agrobacterium sp. - a new enzyme of carnitine metabolism

Hanschmann, H.; Kleber, H.P.; Biochim. Biophys. Acta 1337, 133-142 (1997)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
Carnitine amide
competitive inhibitor of (S)-carnitine oxidation
Agrobacterium sp.
cetyltrimethylammoniumbromide
D-carnitine dehydrogenase, higher than 5 mM, 10% of initial activity
Agrobacterium sp.
choline
competitive inhibitor of (S)-carnitine oxidation; D-carnitine dehydrogenase, competitive inhibition
Agrobacterium sp.
crotonobetaine
competitive inhibitor of (S)-carnitine oxidation; D-carnitine dehydrogenase, competitive inhibition
Agrobacterium sp.
Cu2+
; D-carnitine dehydrogenase, 1 mM, 25-70% inhibition
Agrobacterium sp.
DL-beta-hydroxybutyrate
D-carnitine dehydrogenase, competitive inhibition
Agrobacterium sp.
DL-carnitine amide
D-carnitine dehydrogenase, competitive inhibition
Agrobacterium sp.
EDTA
; D-carnitine dehydrogenase, 20 mM, 25-70% inhibition
Agrobacterium sp.
Fe2+
; D-carnitine dehydrogenase, 1 mM, 25-70% inhibition
Agrobacterium sp.
gamma-butyrobetaine
competitive inhibitor of (S)-carnitine oxidation; D-carnitine dehydrogenase, competitive inhibition
Agrobacterium sp.
glycine betaine
competitive inhibitor of (S)-carnitine oxidation; D-carnitine dehydrogenase, competitive inhibition
Agrobacterium sp.
Hexadecyltrimethylammonium bromide
above 5 mM, 90% loss of activity
Agrobacterium sp.
Hg2+
; D-carnitine dehydrogenase, 0.01 mM, complete inhibition
Agrobacterium sp.
L(-)-carnitine
competitive inhibitor of (S)-carnitine oxidation
Agrobacterium sp.
L-carnitine
D-carnitine dehydrogenase, strong competitive inhibition
Agrobacterium sp.
p-chloromercuribenzoate
; D-carnitine dehydrogenase, 0.01 mM, complete inhibition
Agrobacterium sp.
SDS
above 5 mM, 90% loss of activity; D-carnitine dehydrogenase, higher than 5 mM, 10% of initial activity
Agrobacterium sp.
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.047
-
NADH
; D-carnitine dehydrogenase
Agrobacterium sp.
0.15
-
NAD+
; D-carnitine dehydrogenase
Agrobacterium sp.
1.2
-
3-dehydrocarnitine
; D-carnitine dehydrogenase
Agrobacterium sp.
5.5
-
D-carnitine
D-carnitine dehydrogenase
Agrobacterium sp.
5.5
-
(S)-carnitine
-
Agrobacterium sp.
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Co2+
1 mM, increases activity up to 31%; D-carnitine dehydrogenase, 5 mM, 31% increase in activity
Agrobacterium sp.
Ni2+
5 mM, increases activity up to 31%; D-carnitine dehydrogenase, 5 mM, 31% increase in activity
Agrobacterium sp.
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
28000
-
3 * 28000, D-carnitine dehydrogenase, SDS-PAGE; 3 * 28000, SDS-PAGE, laser-induced mass spectrometry
Agrobacterium sp.
88000
-
gel filtration; gel filtration, D-carnitine dehydrogenase
Agrobacterium sp.
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
Agrobacterium sp.
-
3-dehydrocarnitine + NADH + H+
-
Agrobacterium sp.
r
additional information
Agrobacterium sp.
initial step of D(+)-carnitine degradation
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Agrobacterium sp.
-
; DSM 8888, D-carnitine- and L-carnitine dehydrogenases are induced by D-carnitine and L-carnitine respectively
-
Purification (Commentary)
Commentary
Organism
; DEAE-Sepharose FF, TSK Butyl, Phenyl-Sepharose, Superose 12 HR, D-carnitine dehydrogenase
Agrobacterium sp.
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
14.15
-
; D-carnitine dehydrogenase
Agrobacterium sp.
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
-
9589
Agrobacterium sp.
3-dehydrocarnitine + NADH + H+
-
9589
Agrobacterium sp.
r
(S)-3-hydroxy-4-trimethylaminobutyrate + NAD+
D-carnitine dehydrogenase
9589
Agrobacterium sp.
3-dehydrocarnitine + NADH + H+
-
9589
Agrobacterium sp.
r
(S)-carnitine + NAD+
r
9589
Agrobacterium sp.
3-dehydrocarnitine + NADH + H+
-
9589
Agrobacterium sp.
-
carnitine + NAD+
-
9589
Agrobacterium sp.
3-dehydrocarnitine + NADH + H+
-
9589
Agrobacterium sp.
r
DL-4-amino-3-hydroxy-n-butyrate + NAD+
D-carnitine dehydrogenase, less than 20% velocity compared to D-carnitine
9589
Agrobacterium sp.
DL-4-amino-3-keto-n-butyrate + NADH
-
9589
Agrobacterium sp.
?
additional information
initial step of D(+)-carnitine degradation
9589
Agrobacterium sp.
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
trimer
3 * 28000, D-carnitine dehydrogenase, SDS-PAGE; 3 * 28000, SDS-PAGE, laser-induced mass spectrometry
Agrobacterium sp.
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
; D-carnitine dehydrogenase
Agrobacterium sp.
Temperature Stability [C]
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
40
-
D-carnitine dehydrogenase, enzyme activity decrases rapidly above 40C; rapid decrease of stability above
Agrobacterium sp.
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
5.5
6.5
3-dehydrocarnitine + NADH; D-carnitine dehydrogenase, reduction of D-carnitine
Agrobacterium sp.
9
9.5
D-carnitine dehydrogenase, oxidation of D-carnitine; (S)-carnitine + NAD+
Agrobacterium sp.
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
6
8
D-carnitine dehydrogenase, stable for 100 h at 4C
Agrobacterium sp.
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
; specific for NAD+
Agrobacterium sp.
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
; specific for NAD+
Agrobacterium sp.
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Carnitine amide
competitive inhibitor of (S)-carnitine oxidation
Agrobacterium sp.
cetyltrimethylammoniumbromide
D-carnitine dehydrogenase, higher than 5 mM, 10% of initial activity
Agrobacterium sp.
choline
competitive inhibitor of (S)-carnitine oxidation; D-carnitine dehydrogenase, competitive inhibition
Agrobacterium sp.
crotonobetaine
competitive inhibitor of (S)-carnitine oxidation; D-carnitine dehydrogenase, competitive inhibition
Agrobacterium sp.
Cu2+
; D-carnitine dehydrogenase, 1 mM, 25-70% inhibition
Agrobacterium sp.
DL-beta-hydroxybutyrate
D-carnitine dehydrogenase, competitive inhibition
Agrobacterium sp.
DL-carnitine amide
D-carnitine dehydrogenase, competitive inhibition
Agrobacterium sp.
EDTA
; D-carnitine dehydrogenase, 20 mM, 25-70% inhibition
Agrobacterium sp.
Fe2+
; D-carnitine dehydrogenase, 1 mM, 25-70% inhibition
Agrobacterium sp.
gamma-butyrobetaine
competitive inhibitor of (S)-carnitine oxidation; D-carnitine dehydrogenase, competitive inhibition
Agrobacterium sp.
glycine betaine
competitive inhibitor of (S)-carnitine oxidation; D-carnitine dehydrogenase, competitive inhibition
Agrobacterium sp.
Hexadecyltrimethylammonium bromide
above 5 mM, 90% loss of activity
Agrobacterium sp.
Hg2+
; D-carnitine dehydrogenase, 0.01 mM, complete inhibition
Agrobacterium sp.
L(-)-carnitine
competitive inhibitor of (S)-carnitine oxidation
Agrobacterium sp.
L-carnitine
D-carnitine dehydrogenase, strong competitive inhibition
Agrobacterium sp.
p-chloromercuribenzoate
; D-carnitine dehydrogenase, 0.01 mM, complete inhibition
Agrobacterium sp.
SDS
above 5 mM, 90% loss of activity; D-carnitine dehydrogenase, higher than 5 mM, 10% of initial activity
Agrobacterium sp.
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.047
-
NADH
; D-carnitine dehydrogenase
Agrobacterium sp.
0.15
-
NAD+
; D-carnitine dehydrogenase
Agrobacterium sp.
1.2
-
3-dehydrocarnitine
; D-carnitine dehydrogenase
Agrobacterium sp.
5.5
-
D-carnitine
D-carnitine dehydrogenase
Agrobacterium sp.
5.5
-
(S)-carnitine
-
Agrobacterium sp.
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Co2+
1 mM, increases activity up to 31%; D-carnitine dehydrogenase, 5 mM, 31% increase in activity
Agrobacterium sp.
Ni2+
5 mM, increases activity up to 31%; D-carnitine dehydrogenase, 5 mM, 31% increase in activity
Agrobacterium sp.
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
28000
-
3 * 28000, D-carnitine dehydrogenase, SDS-PAGE; 3 * 28000, SDS-PAGE, laser-induced mass spectrometry
Agrobacterium sp.
88000
-
gel filtration; gel filtration, D-carnitine dehydrogenase
Agrobacterium sp.
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-trimethylaminobutyrate + NAD+
Agrobacterium sp.
-
3-dehydrocarnitine + NADH + H+
-
Agrobacterium sp.
r
additional information
Agrobacterium sp.
initial step of D(+)-carnitine degradation
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
; DEAE-Sepharose FF, TSK Butyl, Phenyl-Sepharose, Superose 12 HR, D-carnitine dehydrogenase
Agrobacterium sp.
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
14.15
-
; D-carnitine dehydrogenase
Agrobacterium sp.
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(R)-3-hydroxy-4-trimethylaminobutyrate + NAD+
-
9589
Agrobacterium sp.
3-dehydrocarnitine + NADH + H+
-
9589
Agrobacterium sp.
r
(S)-3-hydroxy-4-trimethylaminobutyrate + NAD+
D-carnitine dehydrogenase
9589
Agrobacterium sp.
3-dehydrocarnitine + NADH + H+
-
9589
Agrobacterium sp.
r
(S)-carnitine + NAD+
r
9589
Agrobacterium sp.
3-dehydrocarnitine + NADH + H+
-
9589
Agrobacterium sp.
-
carnitine + NAD+
-
9589
Agrobacterium sp.
3-dehydrocarnitine + NADH + H+
-
9589
Agrobacterium sp.
r
DL-4-amino-3-hydroxy-n-butyrate + NAD+
D-carnitine dehydrogenase, less than 20% velocity compared to D-carnitine
9589
Agrobacterium sp.
DL-4-amino-3-keto-n-butyrate + NADH
-
9589
Agrobacterium sp.
?
additional information
initial step of D(+)-carnitine degradation
9589
Agrobacterium sp.
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
trimer
3 * 28000, D-carnitine dehydrogenase, SDS-PAGE; 3 * 28000, SDS-PAGE, laser-induced mass spectrometry
Agrobacterium sp.
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
; D-carnitine dehydrogenase
Agrobacterium sp.
Temperature Stability [C] (protein specific)
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
40
-
D-carnitine dehydrogenase, enzyme activity decrases rapidly above 40C; rapid decrease of stability above
Agrobacterium sp.
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
5.5
6.5
3-dehydrocarnitine + NADH; D-carnitine dehydrogenase, reduction of D-carnitine
Agrobacterium sp.
9
9.5
D-carnitine dehydrogenase, oxidation of D-carnitine; (S)-carnitine + NAD+
Agrobacterium sp.
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
6
8
D-carnitine dehydrogenase, stable for 100 h at 4C
Agrobacterium sp.
Other publictions for EC 1.1.1.254
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)
654037
Kluettermann
-
Synthesis of poly-beta-hydroxy ...
Agrobacterium tumefaciens
Acta Biotechnol.
22
261-269
2002
-
1
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
1
-
1
1
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
285734
Obon
Enzymatic cycling assay for D- ...
Agrobacterium sp.
Anal. Biochem.
274
34-39
1999
-
-
-
-
-
-
-
-
-
-
-
1
-
2
-
-
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
9587
Setyahadi
-
Production of L-carnitine from ...
Agrobacterium sp.
J. Mol. Catal. , B Enzym.
4
205-209
1998
-
-
-
-
-
-
-
-
1
-
-
2
-
1
-
-
1
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
2
-
-
-
1
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
9588
Hanschmann
-
Conversion of D-carnitine into ...
Agrobacterium sp.
Biotechnol. Lett.
19
679-682
1997
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
1
2
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
2
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
9589
Hanschmann
Purification and characterizat ...
Agrobacterium sp.
Biochim. Biophys. Acta
1337
133-142
1997
-
-
-
-
-
-
17
5
-
2
2
2
-
4
-
-
1
-
-
-
1
-
6
1
1
-
1
-
2
-
1
1
-
-
-
-
-
-
1
-
-
-
-
17
-
5
-
2
2
2
-
-
-
1
-
-
1
-
6
1
1
-
1
-
2
-
1
-
-
-
-
-
-
-
285735
Setyahida
Purification and properties of ...
Agrobacterium sp. 525a
Biosci. Biotechnol. Biochem.
61
1055-1058
1997
-
-
-
-
-
-
6
4
-
1
2
1
-
2
-
-
1
-
-
-
1
-
4
1
1
-
1
-
2
-
1
1
-
-
-
-
-
-
1
-
-
-
-
6
-
4
-
1
2
1
-
-
-
1
-
-
1
-
4
1
1
-
1
-
2
-
1
-
-
-
-
-
-
-