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Information on EC 2.3.1.190 - acetoin dehydrogenase system
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2.3.1.190 acetoin dehydrogenase systemIUBMB Comments
Requires thiamine diphosphate. It belongs to the 2-oxoacid dehydrogenase system family, which also includes EC 1.2.1.104, pyruvate dehydrogenase system, EC 1.2.1.105, 2-oxoglutarate dehydrogenase system, EC 1.2.1.25, branched-chain alpha-keto acid dehydrogenase system, and EC 1.4.1.27, glycine cleavage system. With the exception of the glycine cleavage system, which contains 4 components, the 2-oxoacid dehydrogenase systems share a common structure, consisting of three main components, namely a 2-oxoacid dehydrogenase (E1), a dihydrolipoamide acyltransferase (E2), and dihydrolipoamide dehydrogenase (E3).
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Word Map
- 2.3.1.190
- dihydrolipoamide
-
alcaligenes
- carbinolicus
-
catabolite
-
pelobacter
- eutrophus
- magnum
-
dissimilation
- 2,3-butanediol
- synthesis
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
acetoin dehydrogenase, acetoin dehydrogenase enzyme system, ao:dcpip or, aodh es, acetoin dehydrogenase complex, acetoin dehydrogenase e1, pa4150, acetoin dehydrogenase system, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetoin dehydrogenase
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acetoin dehydrogenase complex
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acetoin dehydrogenase E1
acetoin dehydrogenase enzyme system
AcoAB
AoDH ES
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PA4150
PA4151
acetoin dehydrogenase enzyme system
Q9HWN1; Q9HWN0
consists of TPP-dependent acetoin dehydrogenase (AoDH E1), dihydrolipoamide acetyltransferase (AoDH E2) and dihydrolipoamide dehydrogenase (AoDH E3)
acetoin dehydrogenase enzyme system
Q9HWN1; Q9HWN0
consists of TPP-dependent acetoin dehydrogenase (AoDH E1), dihydrolipoamide acetyltransferase (AoDH E2) and dihydrolipoamide dehydrogenase (AoDH E3)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetoin + CoA + NAD+ = acetaldehyde + acetyl-CoA + NADH + H+
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:acetoin O-acetyltransferase
Requires thiamine diphosphate. It belongs to the 2-oxoacid dehydrogenase system family, which also includes EC 1.2.1.104, pyruvate dehydrogenase system, EC 1.2.1.105, 2-oxoglutarate dehydrogenase system, EC 1.2.1.25, branched-chain alpha-keto acid dehydrogenase system, and EC 1.4.1.27, glycine cleavage system. With the exception of the glycine cleavage system, which contains 4 components, the 2-oxoacid dehydrogenase systems share a common structure, consisting of three main components, namely a 2-oxoacid dehydrogenase (E1), a dihydrolipoamide acyltransferase (E2), and dihydrolipoamide dehydrogenase (E3).
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetoin + 2,6-dichlorophenolindophenol
acetaldehyde + ?
E1 complex
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-
?
acetoin + 2,6-dichlorophenolindophenol
acetaldehyde + ?
E1 complex
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-
?
acetoin + CoA + NAD+
acetaldehyde + acetyl-CoA + NADH + H+
Q9HWN1; Q9HWN0
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-
?
acetoin + CoA + NAD+
acetaldehyde + acetyl-CoA + NADH + H+
Q9HWN1; Q9HWN0
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-
?
diacetyl + 2,6-dichlorophenolindophenol
?
E1 complex, 59% of the activity with acetoin
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?
methyl acetoin + 2,6-dichlorophenolindophenol
? + ?
E1 complex, 107% of the activity with acetoin
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?
additional information
?
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no detectable activity with 2-oxoglutarate, pyruvate or the branched-chain 2-oxoacids, 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate
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-
?
additional information
?
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no detectable activity with 2-oxoglutarate, pyruvate or the branched-chain 2-oxoacids, 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate
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-
?
additional information
?
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no detectable activity with 2-oxoglutarate, pyruvate or the branched-chain 2-oxoacids, 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate
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?
additional information
?
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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+
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
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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+
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-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
additional information
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disruption of the gene acoA encoding subunit E1alpha results in strains impaired in expression of dephosphate-dependent E1 activity, to remove acetoin from the medium and to grow with acetoin as sole carbon source
malfunction
Q9HWN1; Q9HWN0
acoA, acoB are knocked out individually in Pseudomonas aeruginosa PAO1. The mutants lose the ability to grow in acetoin or 2,3-butanediol
malfunction
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acoA, acoB are knocked out individually in Pseudomonas aeruginosa PAO1. The mutants lose the ability to grow in acetoin or 2,3-butanediol
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metabolism
Q9HWN1; Q9HWN0
the enzyme is involved in 2,3-butanediol catabolism
metabolism
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the enzyme is involved in the degradation of the sulfonylurea herbicide nicosulfuron
metabolism
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the enzyme is involved in 2,3-butanediol catabolism
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metabolism
Bacillus subtilis YB10
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the enzyme is involved in the degradation of the sulfonylurea herbicide nicosulfuron
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physiological function
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the acetoin dehydrogenase enzyme system is responsible for R-acetoin dissimilation. Mutants lose the ability to grow on acetoin as the sole carbon source, and the acetoin accumulated cannot be dissimilated. In the presence of another carbon source, the acetoin accumulated in broth of acetoin dehydrogenase mutants is converted to 2,3-butanediol
physiological function
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the acetoin dehydrogenase enzyme system is responsible for R-acetoin dissimilation. Mutants lose the ability to grow on acetoin as the sole carbon source, and the acetoin accumulated cannot be dissimilated. In the presence of another carbon source, the acetoin accumulated in broth of acetoin dehydrogenase mutants is converted to 2,3-butanediol
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Show AA Sequence and Transmembrane Helices (169 entries)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
138000
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gel filtration, component E1, i.e. acetoin:2,6-dichlorophenolindophenol oxidoreductase
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
component E1, i.e. acetoin:2,6-dichlorophenolindophenol oxidoreductase, exhibits tetrameric alpha2beta2 structure, with alpha, 35243 Da and beta, 35788 Da, calculated and SDS-PAGE
additional information
component E1, i.e. acetoin:2,6-dichlorophenolindophenol oxidoreductase, exhibits tetrameric alpha2beta2 structure, with alpha, 35243 Da and beta, 35788 Da, calculated and SDS-PAGE
additional information
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component E1, i.e. acetoin:2,6-dichlorophenolindophenol oxidoreductase, exhibits tetrameric alpha2beta2 structure, with alpha, 38500 and beta, 34000 Da, SDS-PAGE
additional information
component E1, i.e. acetoin:2,6-dichlorophenolindophenol oxidoreductase, exhibits tetrameric alpha2beta2 structure, with alpha, 43000 and beta, 33000 Da, SDS-PAGE
additional information
component E1, i.e. acetoin:2,6-dichlorophenolindophenol oxidoreductase, exhibits tetrameric alpha2beta2 structure, with alpha, 43000 and beta, 33000 Da, SDS-PAGE
additional information
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component E1, i.e. acetoin:2,6-dichlorophenolindophenol oxidoreductase, exhibits tetrameric alpha2beta2 structure, with alpha, 43000 and beta, 33000 Da, SDS-PAGE
additional information
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component E1, i.e. acetoin:2,6-dichlorophenolindophenol oxidoreductase, exhibits tetrameric alpha2beta2 structure, with alpha, 37500 Da, and beta, 38500 Da, SDS-PAGE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
from acetoin-grown cells
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
formation of the enzyme components of the acetoin dehydrogenase enzyme system E1, i.e. acetoin:2,6-dichlorophenolindophenol oxidoreductase Ao:DCPIP OR,, E2, i.e. dihydrolipoamide acetyltransferase DHLTA, and E3, i.e. dihydrolipoamide dehydrogenase DHLDH, are induced during growth on acetoin
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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
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transcriptions of the aco operon and acoR are repressed by glucose via CcpA, and CcpA specifically bound to sequences within the acoR promoter fragment
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
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engineering a budC acoABCD double mutant, which has lost 2,3-butanediol dehydrogenase activity and the acetoin dehydrogenase system for R-acetoin production. Optimized conditions include aerobic batch culture and mildly acidic conditions. 62.3 g per l R-acetoin can be produced by budC and acoABCD double mutants in 57 h culture, with an optical purity of 98.0%, and a substrate conversion ratio of 28.7%
synthesis
-
engineering a budC acoABCD double mutant, which has lost 2,3-butanediol dehydrogenase activity and the acetoin dehydrogenase system for R-acetoin production. Optimized conditions include aerobic batch culture and mildly acidic conditions. 62.3 g per l R-acetoin can be produced by budC and acoABCD double mutants in 57 h culture, with an optical purity of 98.0%, and a substrate conversion ratio of 28.7%
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Oppermann, F.B.; Schmidt, B.; Steinbuchel, A.
Purification and characterization of acetoin:2,6-dichlorophenolindophenol oxidoreductase, dihydrolipoamide dehydrogenase, and dihydrolipoamide acetyltransferase of the Pelobacter carbinolicus acetoin dehydrogenase enzyme system
J. Bacteriol.
173
757-767
1991
Syntrophotalea carbinolica
brenda
Lorenzl, H.; Oppermann, F.; Schmidt, B.; Steinbuchel, A.
Purification and characterization of the E1 component of the Clostridium magnum acetoin dehydrogenase enzyme system
Antonie van Leeuwenhoek
64
9-15
1993
Clostridium magnum
brenda
Payne, K.A.; Hough, D.W.; Danson, M.J.
Discovery of a putative acetoin dehydrogenase complex in the hyperthermophilic archaeon Sulfolobus solfataricus
FEBS Lett.
584
1231-1234
2010
Saccharolobus solfataricus (Q97YF5), Saccharolobus solfataricus (Q97YF6), Saccharolobus solfataricus
brenda
Huang, M.; Oppermann, F.B.; Steinbuechel, A.
Molecular characterization of the Pseudomonas putida 2,3-butanediol catabolic pathway
FEMS Microbiol. Lett.
124
141-150
1994
Pseudomonas putida (Q52014), Pseudomonas putida (Q52015), Pseudomonas putida
brenda
Priefert, H.; Hein, S.; Krueger, N.; Zeh, K.; Schmidt, B.; Steinbuechel, A.
Identification and molecular characterization of the Alcaligenes eutrophus H16 aco operon genes involved in acetoin catabolism
J. Bacteriol.
173
4056-4071
1991
Alcaligenes eutrophus H16 (P27745), Alcaligenes eutrophus H16 (P27746)
brenda
Krueger, N.; Oppermann, F.B.; Lorenzl, H.; Steinbuechel, A.
Biochemical and molecular characterization of the Clostridium magnum acetoin dehydrogenase enzyme system
J. Bacteriol.
176
3614-3630
1994
Clostridium magnum (Q46142), Clostridium magnum (Q46143), Clostridium magnum
brenda
Huang, M.; Oppermann-Sanio, F.B.; Steinbuechel, A.
Biochemical and molecular characterization of the Bacillus subtilis acetoin catabolic pathway
J. Bacteriol.
181
3837-3841
1999
Bacillus subtilis
brenda
Wang, D.; Zhou, J.; Chen, C.; Wei, D.; Shi, J.; Jiang, B.; Liu, P.; Hao, J.
R-acetoin accumulation and dissimilation in Klebsiella pneumoniae
J. Ind. Microbiol. Biotechnol.
42
1105-1115
2015
Klebsiella pneumoniae, Klebsiella pneumoniae CGMCC 1.6366
brenda
Liu, Q.; Liu, Y.; Kang, Z.; Xiao, D.; Gao, C.; Xu, P.; Ma, C.
2,3-Butanediol catabolism in Pseudomonas aeruginosa PAO1
Environ. Microbiol.
20
3927-3940
2018
Pseudomonas aeruginosa (Q9HWN1 AND Q9HWN0), Pseudomonas aeruginosa, Pseudomonas aeruginosa ATCC 15692 (Q9HWN1 AND Q9HWN0)
brenda
Zhang, Z.; Zhang, Y.; Yang, D.C.; Zhang, J.L.
Expression and functional analysis of three nicosulfuron-degrading enzymes from Bacillus subtilis YB1
J. Environ. Sci. Health B
53
476-485
2018
Bacillus subtilis, Bacillus subtilis YB10
brenda
Peng, Q.; Zhao, X.; Wen, J.; Huang, M.; Zhang, J.; Song, F.
Transcription in the acetoin catabolic pathway is regulated by AcoR and CcpA in Bacillus thuringiensis
Microbiol. Res.
235
126438
2020
Bacillus thuringiensis
brenda
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