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Information on EC 1.1.1.303 - diacetyl reductase [(R)-acetoin forming]
for references in articles please use BRENDA:EC1.1.1.303
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.303 diacetyl reductase [(R)-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 yeast Saccharomyces cerevisiae [1,2]. Different from EC 1.1.1.304, diacetyl reductase [(S)-acetoin forming].
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
showSynonyms
(R,R)-BDH, (R,R)-butane-2,3-diol dehydrogenase, (R,R)-butanediol dehydrogenase/diacetyl reductase, acetoin/diacetyl reductase, BdhA, DAR, dudA, EC 1.1.1.5, gutB, More, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(R,R)-BDH
(R,R)-butane-2,3-diol dehydrogenase
(R,R)-butanediol dehydrogenase/diacetyl reductase
acetoin/diacetyl reductase
BdhA
DAR
dudA
EC 1.1.1.5
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-
formerly, part transferred
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gutB
additional information
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(R)-acetoin + NAD+ = diacetyl + NADH + H+
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-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
MetaCyc
pyruvate fermentation to (R)-acetoin I
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SYSTEMATIC NAME
IUBMB Comments
(R)-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 yeast Saccharomyces cerevisiae [1,2]. Different from EC 1.1.1.304, diacetyl reductase [(S)-acetoin forming].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,2-cyclohexanedione + NADH + H+
(R)-2-hydroxy-1-cyclohexanone + NAD+
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Substrates: 5% of the (R)-2,3-butanediol dehydrogenase activity with substrate acetoin
Products: -
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2,3-pentanedione + NADH + H+
(3R)-3-hydroxy-2-pentanone + NAD+
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Substrates: 7% of the (R)-2,3-butanediol dehydrogenase activity with substrate acetoin
Products: -
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diacetyl + NADH + H+
(R)-acetoin + NAD+
Substrates: -
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diacetyl + NADH + H+
(R)-acetoin + NAD+
Substrates: stereoselective reduction
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diacetyl + NADH + H+
(R)-acetoin + NAD+
Alkalihalobacillus clausii DSM 8716
Substrates: -
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diacetyl + NADH + H+
(R)-acetoin + NAD+
Alkalihalobacillus clausii DSM 8716
Substrates: stereoselective reduction
Products: -
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diacetyl + NADH + H+
(R)-acetoin + NAD+
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Substrates: 60% activity compared to main activity of 2,3-butanediol dehydrogenase, i.e. oxidation of (2R,3R)-2,3-butanediol and reduction of (R)-acetoin, EC 1.1.1.4
Products: -
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diacetyl + NADH + H+
(R)-acetoin + NAD+
-
Substrates: -
Products: -
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diacetyl + NADH + H+
(R)-acetoin + NAD+
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Substrates: 60% activity compared to main activity of 2,3-butanediol dehydrogenase, i.e. oxidation of (2R,3R)-2,3-butanediol and reduction of (R)-acetoin, EC 1.1.1.4
Products: -
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diacetyl + NADH + H+
(R)-acetoin + NAD+
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Substrates: 21% of the (R)-2,3-butanediol dehydrogenase activity with substrate acetoin
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diacetyl + NADH + H+
(R)-acetoin + NAD+
Substrates: 51.4% of the (R)-2,3-butanediol dehydrogenase activity with substrate acetoin
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ir
additional information
?
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Substrates: the two step reduction of diacetyl (butane-2,3-dione) with (R,R)-BDH solely yields (R,R)-butane-2,3-diol via (R)-acetoin, cf. EC 1.1.1.4. The enzyme catalyzes the (R)-specific oxidation of (R,R)- and meso-butane-2,3-diol to (R)- and (S)-acetoin with specific activities of 12 U/mg and 23 U/mg, respectively. Starting with diacetyl as a substrate, exclusively (R,R)-butane-2,3-diol is formed. Bacillus clausii BDH catalyzes a highly selective oxidation of secondary alcohol groups in (R)-configuration of butane-2,3-diols and also reduces the carbonyl function in acetoin and diacetyl in a stereoselective manner to yield the (R)-configuration of the resulting chiral center, it selectively acts on vicinal diketones, alpha-hydroxy ketones and vicinal diols
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additional information
?
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Alkalihalobacillus clausii DSM 8716
Substrates: the two step reduction of diacetyl (butane-2,3-dione) with (R,R)-BDH solely yields (R,R)-butane-2,3-diol via (R)-acetoin, cf. EC 1.1.1.4. The enzyme catalyzes the (R)-specific oxidation of (R,R)- and meso-butane-2,3-diol to (R)- and (S)-acetoin with specific activities of 12 U/mg and 23 U/mg, respectively. Starting with diacetyl as a substrate, exclusively (R,R)-butane-2,3-diol is formed. Bacillus clausii BDH catalyzes a highly selective oxidation of secondary alcohol groups in (R)-configuration of butane-2,3-diols and also reduces the carbonyl function in acetoin and diacetyl in a stereoselective manner to yield the (R)-configuration of the resulting chiral center, it selectively acts on vicinal diketones, alpha-hydroxy ketones and vicinal diols
Products: -
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additional information
?
-
-
Substrates: enzyme is specific for NADH
Products: -
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
diacetyl + NADH + H+
(R)-acetoin + NAD+
Substrates: -
Products: -
Products: -
ir
diacetyl + NADH + H+
(R)-acetoin + NAD+
Alkalihalobacillus clausii DSM 8716
Substrates: -
Products: -
Products: -
ir
diacetyl + NADH + H+
(R)-acetoin + NAD+
-
Substrates: -
Products: -
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ir
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
diacetyl
slight substrate inhibition, physiologically irrelevant
dipicolinate
-
inhibition, (R)-2,3-butanediol dehydrogenase activity
o-phenanthroline
-
inhibition, (R)-2,3-butanediol dehydrogenase activity
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Michaelis-Menten kinetics, Arrhenius plots permit the calculation of activation energies of 27 kJ/mol, 41 kJ/mol and 60 kJ/mol for the BDH catalyzed acetoin reductase, diacetyl reductase and butane-2,3-diol dehydrogenase activities, respectively
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
the pH-dependence of diacetyl reduction behaves quite differently from the acetoin reductase activity (optimum pH 7.0). The pH optimum is shifted down to pH 6.0, and the pH-dependence of activity is narrower as compared to the acetoin reductase activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
acetoin reductase, diacetyl reductase and butane-2,3-diol dehydrogenase activities show temperature optima at 50°C
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional diacetyl reductase and (R)-2,3-butanediol dehydrogenase
-
-
brenda
bifunctional diacetyl reductase and (R)-2,3-butanediol dehydrogenase
UniProt
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
gene disruption is not lethal. Disrupted strains can grow on 2,3-butanediol, but to a lesser cell density than wild-type
physiological function
dudA, the gene encoding DAR, is the key factor responsible for the formation of meso-2,3-butanediol
physiological function
-
the enzyme is a 2,3-butanediol dehydrogenase (BDH, EC 1.1.1.4) and also a acetoin/diacetyl reductase, that catalyzes the stereospecific oxidation of (2R,3R)-2,3-butanediol and the reverse reduction of (R)-acetoin to (2R,3R)-2,3-butanediol, as well as the reduction of diacetyl to (R)-acetoin. It is a pivotal enzyme for the formation of 2,3-butanediol (2,3-BD), a chiral compound with potential roles in the virulence of certain pathogens
physiological function
-
the enzyme is a 2,3-butanediol dehydrogenase (BDH, EC 1.1.1.4) and also a acetoin/diacetyl reductase, that catalyzes the stereospecific oxidation of (2R,3R)-2,3-butanediol and the reverse reduction of (R)-acetoin to (2R,3R)-2,3-butanediol, as well as the reduction of diacetyl to (R)-acetoin. It is a pivotal enzyme for the formation of 2,3-butanediol (2,3-BD), a chiral compound with potential roles in the virulence of certain pathogens
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physiological function
-
dudA, the gene encoding DAR, is the key factor responsible for the formation of meso-2,3-butanediol
-
Show AA Sequence and Transmembrane Helices (250 entries)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
knockout of diacetyl reductase (DAR) gene dudA in Paenibacillus polymyxa strain ZJ-9 via homologous recombination between the genome and the previously constructed targeting vector pRN5101-L'C in a process based on homologous single-crossover. Disruption mutant Paenibacillus polymyxa ZJ-9-DELTAdudA is used for production of (R,R)-2,3-butanediol of ultra-high optical purity, and without parts of meso-2,3-butanediol, through (R,R)-butanediol dehydrogenase (EC 1.1.1.4). Paenibacillus polymyxa is a microorganism with a reported potential for the industrial production of (R,R)-2,3-butanediol. Gene dudA, the gene encoding DAR, is the key factor responsible for the formation of meso-2,3-butanediol, thus reducing the purity of (R,R)-2,3-butanediol
additional information
-
knockout of diacetyl reductase (DAR) gene dudA in Paenibacillus polymyxa strain ZJ-9 via homologous recombination between the genome and the previously constructed targeting vector pRN5101-L'C in a process based on homologous single-crossover. Disruption mutant Paenibacillus polymyxa ZJ-9-DELTAdudA is used for production of (R,R)-2,3-butanediol of ultra-high optical purity, and without parts of meso-2,3-butanediol, through (R,R)-butanediol dehydrogenase (EC 1.1.1.4). Paenibacillus polymyxa is a microorganism with a reported potential for the industrial production of (R,R)-2,3-butanediol. Gene dudA, the gene encoding DAR, is the key factor responsible for the formation of meso-2,3-butanediol, thus reducing the purity of (R,R)-2,3-butanediol
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Heidlas, J.; Tressl, R.
Purification and characterization of a (R)-2,3-butanediol dehydrogenase from Saccharomyces cerevisiae
Arch. Microbiol.
154
267-273
1990
Saccharomyces cerevisiae
brenda
Gonzalez, E.; Fernandez, M.R.; Larroy, C.; Sola, L.; Pericas, M.A.; Pares, X.; Biosca, J.A.
Characterization of a (2R,3R)-2,3-butaendiol dehydrogenase as the Saccharomyces cerevisiae YAL060W gene product
J. Biol. Chem.
275
35876-35885
2000
Saccharomyces cerevisiae (P39714)
brenda
Zhang, L.; Cao, C.; Jiang, R.; Xu, H.; Xue, F.; Huang, W.; Ni, H.; Gao, J.
Production of R,R-2,3-butanediol of ultra-high optical purity from Paenibacillus polymyxa ZJ-9 using homologous recombination
Biores. Technol.
261
272-278
2018
Paenibacillus polymyxa (V9NF79), Paenibacillus polymyxa ZJ-9 (V9NF79)
brenda
Muschallik, L.; Molinnus, D.; Bongaerts, J.; Pohl, M.; Wagner, T.; Schoening, M.; Siegert, P.; Selmer, T.
(R,R)-Butane-2,3-diol dehydrogenase from Bacillus clausii DSM 8716T cloning and expression of the bdhA-gene, and initial characterization of enzyme
J. Biotechnol.
258
41-50
2017
Alkalihalobacillus clausii (A0A223LRZ7), Alkalihalobacillus clausii DSM 8716 (A0A223LRZ7)
brenda
Tang, W.; Lian, C.; Si, Y.; Chang, J.
Purification and characterization of (2R,3R)-2,3-butanediol dehydrogenase of the human pathogen Neisseria gonorrhoeae FA1090 produced in Escherichia coli
Mol. Biotechnol.
63
491-501
2021
Neisseria gonorrhoeae, Neisseria gonorrhoeae FA1090
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.303)
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