BRENDA - Enzyme Database show
show all sequences of 2.3.1.190

Purification and characterization of acetoin:2,6-dichlorophenolindophenol oxidoreductase, dihydrolipoamide dehydrogenase, and dihydrolipoamide acetyltransferase of the Pelobacter carbinolicus acetoin dehydrogenase enzyme system

Oppermann, F.B.; Schmidt, B.; Steinbuchel, A.; J. Bacteriol. 173, 757-767 (1991)

Data extracted from this reference:

Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
143000
177000
gel filtration
Pelobacter carbinolicus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Pelobacter carbinolicus
The combination of purified Ao:DCPIP OR, dihydrolipoamide dehydrogenase, and dihydrolipoamide acetyltransferase in the presence of thiamine diphosphate and the substrate acetoin or methylacetoin results in a coenzyme A-dependent reduction of NAD+
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pelobacter carbinolicus
-
-
-
Purification (Commentary)
Commentary
Organism
from acetoin-grown cells
Pelobacter carbinolicus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
acetoin + 2,6-dichlorophenolindophenol
-
486168
Pelobacter carbinolicus
acetaldehyde + ?
-
-
-
?
diacetyl + 2,6-dichlorophenolindophenol
-
486168
Pelobacter carbinolicus
?
-
-
-
?
methyl acetoin + 2,6-dichlorophenolindophenol
-
486168
Pelobacter carbinolicus
? + ?
-
-
-
?
additional information
The combination of purified Ao:DCPIP OR, dihydrolipoamide dehydrogenase, and dihydrolipoamide acetyltransferase in the presence of thiamine diphosphate and the substrate acetoin or methylacetoin results in a coenzyme A-dependent reduction of NAD+
486168
Pelobacter carbinolicus
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
More
component E1, i.e. acetoin:2,6-dichlorophenolindophenol oxidoreductase, exhibits tetrameric alpha2beta2 structure, with alpha, 37500 Da, and beta, 38500 Da, SDS-PAGE
Pelobacter carbinolicus
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
143000
177000
gel filtration
Pelobacter carbinolicus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Pelobacter carbinolicus
The combination of purified Ao:DCPIP OR, dihydrolipoamide dehydrogenase, and dihydrolipoamide acetyltransferase in the presence of thiamine diphosphate and the substrate acetoin or methylacetoin results in a coenzyme A-dependent reduction of NAD+
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
from acetoin-grown cells
Pelobacter carbinolicus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
acetoin + 2,6-dichlorophenolindophenol
-
486168
Pelobacter carbinolicus
acetaldehyde + ?
-
-
-
?
diacetyl + 2,6-dichlorophenolindophenol
-
486168
Pelobacter carbinolicus
?
-
-
-
?
methyl acetoin + 2,6-dichlorophenolindophenol
-
486168
Pelobacter carbinolicus
? + ?
-
-
-
?
additional information
The combination of purified Ao:DCPIP OR, dihydrolipoamide dehydrogenase, and dihydrolipoamide acetyltransferase in the presence of thiamine diphosphate and the substrate acetoin or methylacetoin results in a coenzyme A-dependent reduction of NAD+
486168
Pelobacter carbinolicus
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
More
component E1, i.e. acetoin:2,6-dichlorophenolindophenol oxidoreductase, exhibits tetrameric alpha2beta2 structure, with alpha, 37500 Da, and beta, 38500 Da, SDS-PAGE
Pelobacter carbinolicus
Expression
Organism
Commentary
Expression
Pelobacter carbinolicus
the enzymes Ao:DCPIP OR, dihydrolipoamide dehydrogenase, and dihydrolipoamide acetyltransferase are induced during growth on acetoin, whereas they are absent or scarcely present in cells grown on a nonacetoinogenic substrate
up
Expression (protein specific)
Organism
Commentary
Expression
Pelobacter carbinolicus
the enzymes Ao:DCPIP OR, dihydrolipoamide dehydrogenase, and dihydrolipoamide acetyltransferase are induced during growth on acetoin, whereas they are absent or scarcely present in cells grown on a nonacetoinogenic substrate
up
Other publictions for EC 2.3.1.190
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)
736592
Wang
R-acetoin accumulation and dis ...
Klebsiella pneumoniae, Klebsiella pneumoniae CGMCC 1.6366
J. Ind. Microbiol. Biotechnol.
42
1105-1115
2015
-
1
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
703733
Payne
Discovery of a putative acetoi ...
Saccharolobus solfataricus
FEBS Lett.
584
1231-1234
2010
-
-
1
-
-
-
-
1
-
-
1
-
-
7
-
-
-
-
-
-
-
-
8
1
1
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
2
-
-
2
-
-
-
-
-
-
-
-
-
8
2
2
-
-
-
-
-
-
-
-
-
-
-
-
-
704260
Huang
Biochemical and molecular char ...
Bacillus subtilis
J. Bacteriol.
181
3837-3841
1999
-
-
1
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
703742
Huang
Molecular characterization of ...
Pseudomonas putida
FEMS Microbiol. Lett.
124
141-150
1994
-
-
-
-
-
-
-
-
-
-
2
-
-
8
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
704250
Krueger
Biochemical and molecular char ...
Clostridium magnum
J. Bacteriol.
176
3614-3630
1994
-
-
1
-
-
-
-
-
-
-
2
-
-
6
-
-
-
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
1
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
701753
Lorenzl
Purification and characterizat ...
Clostridium magnum
Antonie van Leeuwenhoek
64
9-15
1993
-
-
-
-
-
-
-
-
-
-
1
-
-
4
-
-
1
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
1
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
1
-
-
486168
Oppermann
Purification and characterizat ...
Pelobacter carbinolicus
J. Bacteriol.
173
757-767
1991
-
-
-
-
-
-
-
-
-
-
1
1
-
8
-
-
1
-
-
-
-
-
4
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
1
-
-
-
-
4
1
-
-
-
-
-
-
-
-
1
-
-
1
-
-
704245
Priefert
Identification and molecular c ...
Alcaligenes eutrophus H16
J. Bacteriol.
173
4056-4071
1991
-
-
-
-
-
-
-
-
-
-
1
-
-
4
-
-
1
-
-
-
1
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
2
-
-
2
-
2
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-