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Information on EC 1.1.1.304 - diacetyl reductase [(S)-acetoin forming]
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EC Tree
1.1.1.304 diacetyl reductase [(S)-acetoin forming]IUBMB Comments
The reaction is catalysed in the reverse direction. This activity is usually associated with butanediol dehydrogenase activity (EC 1.1.1.4 or EC 1.1.1.76). While the butanediol dehydrogenase activity is reversible, diacetyl reductase activity is irreversible. This enzyme has been reported in the bacteria Geobacillus stearothermophilus, Enterobacter aerogenes and Klebsiella pneumoniae [1-3]. Different from EC 1.1.1.303, diacetyl reductase [(R)-acetoin forming].
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Word Map
- 1.1.1.304
- lactis
-
alpha-dicarbonyls
- 2,3-pentanedione
- pigeon
- l-xylulose
- xylitol
- alpha-acetolactate
- diacetylactis
-
lager
-
s-acetoin
- synthesis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
diacetyl reductase, ppdar, ardii, readr, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetoin(diacetyl) reductase
AdR
ADS1
BSDR
budC
DAR
diacetyl reductase
EC 1.1.1.5
-
-
formerly, part transferred
-
Kpdar
ReADR
S-stereospecific diacetyl reductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(S)-acetoin + NAD+ = diacetyl + NADH + H+
-
-
-
-
(S)-acetoin + NAD+ = diacetyl + NADH + H+
Theorell-Chance mechanism with NADH as the leading substrate
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
(S)-acetoin:NAD+ oxidoreductase
The reaction is catalysed in the reverse direction. This activity is usually associated with butanediol dehydrogenase activity (EC 1.1.1.4 or EC 1.1.1.76). While the butanediol dehydrogenase activity is reversible, diacetyl reductase activity is irreversible. This enzyme has been reported in the bacteria Geobacillus stearothermophilus, Enterobacter aerogenes and Klebsiella pneumoniae [1-3]. Different from EC 1.1.1.303, diacetyl reductase [(R)-acetoin forming].
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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
(3S)-acetoin + NADH + H+
(2S,3S)-2,3-butanediol + NAD+
-
97% of the activity with diacetyl
97.3% enantiomeric excess and 96.5% diastereomeric excess
-
r
1,2-propanediol + NAD+
? + NADH + H+
-
-
0.5% of the activity with 2,3-butanediol
-
r
2,3-hexanedione + NADH + H+
? + NAD+
-
-
66% of the activity with diacetyl
-
?
2,3-pentanedione + beta-NADH + H+
L-3-hydroxy-2-pentanone + beta-NAD+
-
-
-
-
ir
2,3-pentanedione + NADH + H+
? + NAD+
-
-
69% of the activity with diacetyl
-
?
3,4-hexanedione + NADH + H+
? + NAD+
-
-
10% of the activity with diacetyl
-
?
diacetyl + beta-NADH + H+
(S)-acetoin + beta-NAD+
-
86.9% of the activity with pentane-2,3-dione
-
-
ir
diacetyl + NADH + H+
(3S)-acetoin + NAD+
-
-
97.3% enantiomeric excess
-
ir
ethyl pyruvate + beta-NADH + H+
? + beta-NAD+
-
38.4% of the activity with pentane-2,3-dione
-
-
ir
ethyl pyruvate + NADH + H+
? + NAD+
-
57.7% of the activity with diacetyl
-
-
?
methyl glyoxal + NADH + H+
? + NAD+
-
11% of the activity with diacetyl
-
-
?
methyl pyruvate + beta-NADH + H+
? + beta-NAD+
-
22.8% of the activity with pentane-2,3-dione
-
-
ir
methyl pyruvate + NADH + H+
? + NAD+
-
49% of the activity with diacetyl
-
-
?
2,3-pentanedione + NADH + H+
3-hydroxy-2-pentanone + NAD+
-
85.6% of the activity with diacetyl
-
-
?
2,3-pentanedione + NADH + H+
3-hydroxy-2-pentanone + NAD+
77% of the (R)-2,3-butanediol dehydrogenase activity with substrate acetoin
-
-
?
diacetyl + NADH + H+
(S)-acetoin + NAD+
stereospecific reaction
-
-
?
diacetyl + NADH + H+
(S)-acetoin + NAD+
87% of the (R)-2,3-butanediol dehydrogenase activity with substrate acetoin
-
-
?
additional information
?
-
-
enzyme shows oxidative activity to racemic 2,3-butanediol but no activity toward racemic acetoin in the presence of NAD+
-
-
?
additional information
?
-
-
the enzyme shows an S-enantioselectivity in the reversible reduction of acetoin so it might be responsible of the meso-butenediol formation from R-acetoin. It acts on racemic acetoin and (S)-acetoin to form (2S,3S)-butane-2,3-diol, EC 1.1.1.76, but also on the (2R,3R)-butane-2,3-diol isomer in the reverse reaction, EC 1.1.1.4
-
-
?
additional information
?
-
-
the enzyme shows an S-enantioselectivity in the reversible reduction of acetoin so it might be responsible of the meso-butenediol formation from R-acetoin. It acts on racemic acetoin and (S)-acetoin to form (2S,3S)-butane-2,3-diol, EC 1.1.1.76, but also on the (2R,3R)-butane-2,3-diol isomer in the reverse reaction, EC 1.1.1.4
-
-
?
additional information
?
-
KpDAR has clear activities towards diacetyl, (R)/(S)-acetoin (cf. EC 1.1.1.303) and meso-2,3-butanediol with NADH/NAD+ as the cofactor. Diacetyl is the best substrate in the ketone reduction reactions. meso-2,3-Butanediol is the best substrate in the alcohol oxidation reactions, while very low activity is observed with (R)/(S)-acetoin, (2S,3S)-2,3-butanediol (EC 1.1.1.76) and (2R,3R)-2,3-butanediol (EC 1.1.1.4). Optimization of the reaction conditions, overview. Chiral-column GC analyses of products produced by whole-cells of recombinant Escherichia coli
-
-
-
additional information
?
-
the enzyme BudC also catalyzes the reduction of acetoin by NADH, cf. EC 1.1.1.76
-
-
-
additional information
?
-
enzyme shows activity as a reductase specific for (S)-acetoin, EC 1.1.1.76, and both diacetyl reductase (EC 1.1.1.304) and NAD+-dependent alcohol dehydrogenase (EC 1.1.1.1) activities
-
-
?
additional information
?
-
-
enzyme shows activity as a reductase specific for (S)-acetoin, EC 1.1.1.76, and both diacetyl reductase (EC 1.1.1.304) and NAD+-dependent alcohol dehydrogenase (EC 1.1.1.1) activities
-
-
?
additional information
?
-
KC505218
the enzyme also catalyzes the stereospcific reaction of (S)-acetoin reduction to butanediol, EC 1.1.1.76
-
-
?
additional information
?
-
-
the enzyme also catalyzes the stereospcific reaction of (S)-acetoin reduction to butanediol, EC 1.1.1.76
-
-
?
additional information
?
-
KC505218
the enzyme also catalyzes the stereospcific reaction of (S)-acetoin reduction to butanediol, EC 1.1.1.76
-
-
?
additional information
?
-
-
the enzyme also catalyzes the stereospcific reaction of (S)-acetoin reduction to butanediol, EC 1.1.1.76
-
-
?
additional information
?
-
-
Rhodococcus erythropolis WZ010 is capable of producing optically pure (2S,3S)-2,3-butanediol in alcoholic fermentation.
-
-
?
additional information
?
-
Rhodococcus erythropolis WZ010 is capable of producing optically pure (2S,3S)-2,3-butanediol in alcoholic fermentation.
-
-
?
additional information
?
-
-
the enzyme displays absolute stereospecificity in the reduction of diacetyl to (2S,3S)-2,3-butanediol via (S)-acetoin. The enzyme shows higher catalytic efficiency for (S)-1-phenylethanol oxidation than that for acetophenone reduction. ReADR-catalyzed asymmetric reduction of diacetyl is coupled with stereoselective oxidation of 1-phenylethanol, which simultaneously forms both (2S,3S)-2,3-butanediol and (R)-1-phenylethanol in great conversions and enantiomeric excess values.The enzyme accepts a broad range of substrates including aliphatic and aryl alcohols, aldehydes, and ketones
-
-
?
additional information
?
-
the enzyme displays absolute stereospecificity in the reduction of diacetyl to (2S,3S)-2,3-butanediol via (S)-acetoin. The enzyme shows higher catalytic efficiency for (S)-1-phenylethanol oxidation than that for acetophenone reduction. ReADR-catalyzed asymmetric reduction of diacetyl is coupled with stereoselective oxidation of 1-phenylethanol, which simultaneously forms both (2S,3S)-2,3-butanediol and (R)-1-phenylethanol in great conversions and enantiomeric excess values.The enzyme accepts a broad range of substrates including aliphatic and aryl alcohols, aldehydes, and ketones
-
-
?
additional information
?
-
-
Rhodococcus erythropolis WZ010 is capable of producing optically pure (2S,3S)-2,3-butanediol in alcoholic fermentation.
-
-
?
additional information
?
-
-
the enzyme displays absolute stereospecificity in the reduction of diacetyl to (2S,3S)-2,3-butanediol via (S)-acetoin. The enzyme shows higher catalytic efficiency for (S)-1-phenylethanol oxidation than that for acetophenone reduction. ReADR-catalyzed asymmetric reduction of diacetyl is coupled with stereoselective oxidation of 1-phenylethanol, which simultaneously forms both (2S,3S)-2,3-butanediol and (R)-1-phenylethanol in great conversions and enantiomeric excess values.The enzyme accepts a broad range of substrates including aliphatic and aryl alcohols, aldehydes, and ketones
-
-
?
additional information
?
-
-
no activity with alpha-NADH or NADPH
-
-
?
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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
?
-
-
the enzyme shows an S-enantioselectivity in the reversible reduction of acetoin so it might be responsible of the meso-butenediol formation from R-acetoin. It acts on racemic acetoin and (S)-acetoin to form (2S,3S)-butane-2,3-diol, EC 1.1.1.76, but also on the (2R,3R)-butane-2,3-diol isomer in the reverse reaction, EC 1.1.1.4
-
-
?
additional information
?
-
-
the enzyme shows an S-enantioselectivity in the reversible reduction of acetoin so it might be responsible of the meso-butenediol formation from R-acetoin. It acts on racemic acetoin and (S)-acetoin to form (2S,3S)-butane-2,3-diol, EC 1.1.1.76, but also on the (2R,3R)-butane-2,3-diol isomer in the reverse reaction, EC 1.1.1.4
-
-
?
additional information
?
-
KC505218
the enzyme also catalyzes the stereospcific reaction of (S)-acetoin reduction to butanediol, EC 1.1.1.76
-
-
?
additional information
?
-
-
the enzyme also catalyzes the stereospcific reaction of (S)-acetoin reduction to butanediol, EC 1.1.1.76
-
-
?
additional information
?
-
KC505218
the enzyme also catalyzes the stereospcific reaction of (S)-acetoin reduction to butanediol, EC 1.1.1.76
-
-
?
additional information
?
-
-
the enzyme also catalyzes the stereospcific reaction of (S)-acetoin reduction to butanediol, EC 1.1.1.76
-
-
?
additional information
?
-
-
Rhodococcus erythropolis WZ010 is capable of producing optically pure (2S,3S)-2,3-butanediol in alcoholic fermentation.
-
-
?
additional information
?
-
Rhodococcus erythropolis WZ010 is capable of producing optically pure (2S,3S)-2,3-butanediol in alcoholic fermentation.
-
-
?
additional information
?
-
-
Rhodococcus erythropolis WZ010 is capable of producing optically pure (2S,3S)-2,3-butanediol in alcoholic fermentation.
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
addition of EDTA or the cations at 1 mM, such as Na+, K+, Mn2+, Mg2+, and Ca2+, have no significant effect on the activity of ReADR
additional information
addition of EDTA or the cations at 1 mM, such as Na+, K+, Mn2+, Mg2+, and Ca2+, have no significant effect on the activity of ReADR
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ag+
-
1 mM, 0.5% of initial activity with substrate diacetyl, 0.5% with substrate 2,3-butanediol, respectively
Cu2+
-
1 mM, 0.2% of initial activity with substrate diacetyl, 1% with substrate 2,3-butanediol, respectively
EDTA
-
1 mM, 91% of initial activity with substrate diacetyl, 90% with substrate 2,3-butanediol, respectively
Fe3+
-
1 mM, 2% of initial activity with substrate diacetyl, 3.5% with substrate 2,3-butanediol, respectively
Methyl pyruvate
-
substrate inhibition at concentrations above 80-90 mM
Al3+
-
1 mM, 4% of initial activity with substrate diacetyl, 6% with substrate 2,3-butanediol, respectively
Zn2+
-
1 mM, 75% of initial activity with substrate diacetyl, 80% with substrate 2,3-butanediol, respectively
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
DMSO
DMSO at a final concentration of 30% v/v added into the assay mixture, increases the activity up to 120% of the control enzyme activity
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Neoplasms
Predictors of microscopic portal vein invasion by hepatocellular carcinoma: measurement of portal perfusion defect area ratio.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Michaelis-Menten-type kinetics
-
additional information
additional information
Michaelis-Menten-type kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
79
pH 6.5, temperature not specified in the publication, with FDH
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.8