Information on EC 2.3.1.190 - acetoin dehydrogenase

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The expected taxonomic range for this enzyme is: Bacteria, Archaea

EC NUMBER
COMMENTARY
2.3.1.190
-
RECOMMENDED NAME
GeneOntology No.
acetoin dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
acetoin + CoA + NAD+ = acetaldehyde + acetyl-CoA + NADH + H+
show the reaction diagram
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PATHWAY
KEGG Link
MetaCyc Link
acetoin degradation
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:acetoin O-acetyltransferase
Requires thiamine diphosphate. This enzyme, which belongs to the family of 2-oxo acid dehydrogenase complexes, catalyses the oxidative-hydrolytic cleavage of acetoin to acetaldehyde and acetyl-CoA in many bacterial strains, both aerobic and anaerobic. The enzyme is composed of multiple copies of three enzymic components: acetoin oxidoreductase (E1), dihydrolipoamide acetyltransferase (E2) and dihydrolipoyl dehydrogenase (E3).
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
AcoA
Q52014
-
AcoB
Q52015
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ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Alcaligenes eutrophus H16
subunit acoA
UniProt
Manually annotated by BRENDA team
Alcaligenes eutrophus H16
subunit acoB
UniProt
Manually annotated by BRENDA team
subunit E1alpha
UniProt
Manually annotated by BRENDA team
subunit E1beta
UniProt
Manually annotated by BRENDA team
subunit E1alpha
UniProt
Manually annotated by BRENDA team
subunit E1beta
UniProt
Manually annotated by BRENDA team
E1alpha subunit
UniProt
Manually annotated by BRENDA team
E1beta subunit
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetoin + 2,6-dichlorophenolindophenol
acetaldehyde + ?
show the reaction diagram
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-
-
-
?
acetoin + 2,6-dichlorophenolindophenol
acetaldehyde + ?
show the reaction diagram
Q97YF5, Q97YF6, -
E1 complex
-
-
?
acetoin + 2,6-dichlorophenolindophenol
acetaldehyde + ?
show the reaction diagram
Alcaligenes eutrophus H16
P27745, P27746
E1 complex
-
-
?
diacetyl + 2,6-dichlorophenolindophenol
?
show the reaction diagram
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-
-
-
?
diacetyl + 2,6-dichlorophenolindophenol
?
show the reaction diagram
Q97YF5, Q97YF6, -
E1 complex, 59% of the activity with acetoin
-
-
?
methyl acetoin + 2,6-dichlorophenolindophenol
? + ?
show the reaction diagram
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?
methyl acetoin + 2,6-dichlorophenolindophenol
? + ?
show the reaction diagram
Q97YF5, Q97YF6, -
E1 complex, 107% of the activity with acetoin
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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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additional information
?
-
Q97YF5, Q97YF6, -
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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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
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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COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
thiamine diphosphate
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KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0028
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acetoin
Q97YF5, Q97YF6, -
E1 complex, 80°C, pH 7.0; E1 complex, 80°C, pH 7.0
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2.15
-
Alcaligenes eutrophus H16
P27745, P27746
;
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
80
85
Q97YF5, Q97YF6, -
;
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
136000
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Alcaligenes eutrophus H16
P27745, P27746
gel filtration; gel filtration
138000
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gel filtration, component E1, i.e. acetoin:2,6-dichlorophenolindophenol oxidoreductase
142000
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Q97YF5, Q97YF6, -
gel filtration, E1 complex; gel filtration, E1 complex
143000
177000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-, Q52014, Q52015
x * 34639, calculated; x * 37267, calculated
?
Q46142, Q46143
x * 35532, subunit E1alpha, calculated; x * 35541, subunit E1beta, calculated
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
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
Q97YF5, Q97YF6, -
component E1, i.e. acetoin:2,6-dichlorophenolindophenol oxidoreductase, exhibits tetrameric alpha2beta2 structure, with alpha, 43000 and beta, 33000 Da, SDS-PAGE; component E1, i.e. acetoin:2,6-dichlorophenolindophenol oxidoreductase, exhibits tetrameric alpha2beta2 structure, with alpha, 43000 and beta, 33000 Da, SDS-PAGE
additional information
Alcaligenes eutrophus H16
P27745, P27746
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; 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
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
from acetoin-grown cells; from acetoin-grown cells
Alcaligenes eutrophus H16
P27745, P27746
component E1, i.e. acetoin:2,6-dichlorophenolindophenol oxidoreductase
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from acetoin-grown cells
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Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
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expression in Escherichia coli; expression in Escherichia coli
Q46142, Q46143
component E1alpha; component E1beta
Q97YF5, Q97YF6, -
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
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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