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EC Tree
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, Eukaryota, Archaea
Synonyms
acetoin(diacetyl) reductase, AdR,
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acetoin(diacetyl) reductase
acetoin(diacetyl) reductase
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acetoin(diacetyl) reductase
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AdR
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(R)-acetoin + NAD+ = diacetyl + NADH + H+
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(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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1,2-cyclohexanedione + NADH + H+
(R)-2-hydroxy-1-cyclohexanone + NAD+
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5% of the (R)-2,3-butanediol dehydrogenase activity with substrate acetoin
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ir
2,3-pentanedione + NADH + H+
(3R)-3-hydroxy-2-pentanone + NAD+
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7% of the (R)-2,3-butanediol dehydrogenase activity with substrate acetoin
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ir
diacetyl + NADH + H+
(R)-acetoin + NAD+
additional information
?
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enzyme is specific for NADH
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diacetyl + NADH + H+
(R)-acetoin + NAD+
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r
diacetyl + NADH + H+
(R)-acetoin + NAD+
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r
diacetyl + NADH + H+
(R)-acetoin + NAD+
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21% of the (R)-2,3-butanediol dehydrogenase activity with substrate acetoin
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ir
diacetyl + NADH + H+
(R)-acetoin + NAD+
51.4% of the (R)-2,3-butanediol dehydrogenase activity with substrate acetoin
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ir
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diacetyl + NADH + H+
(R)-acetoin + NAD+
diacetyl + NADH + H+
(R)-acetoin + NAD+
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r
diacetyl + NADH + H+
(R)-acetoin + NAD+
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r
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NADH
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enzyme is specific for NADH
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dipicolinate
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inhibition, (R)-2,3-butanediol dehydrogenase activity
EDTA
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inhibition, (R)-2,3-butanediol dehydrogenase activity
o-phenanthroline
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inhibition, (R)-2,3-butanediol dehydrogenase activity
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Mg2+
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activation, (R)-2,3-butanediol dehydrogenase activity
Mn2+
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activation, (R)-2,3-butanediol dehydrogenase activity
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additional information
additional information
Michaelis-Menten-type kinetics
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gene adr
UniProt
brenda
gene adr
UniProt
brenda
bifunctional diacetyl reductase and (R)-2,3-butanediol dehydrogenase
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brenda
bifunctional diacetyl reductase and (R)-2,3-butanediol dehydrogenase
UniProt
brenda
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physiological function
gene disruption is not lethal. Disrupted strains can grow on 2,3-butanediol, but to a lesser cell density than wild-type
evolution
the enzyme belongs to the family of the short-chain dehydrogenase/reductases
evolution
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the enzyme belongs to the family of the short-chain dehydrogenase/reductases
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35000
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4 * 35000, SDS-PAGE
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tetramer
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4 * 35000, SDS-PAGE
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gene adr, DNA and amino acid sequence determination and analysis, sequence comparison
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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
Wang, Z.; Song, Q.; Yu, M.; Wang, Y.; Xiong, B.; Zhang, Y.; Zheng, J.; Ying, X.
Characterization of a stereospecific acetoin(diacetyl) reductase from Rhodococcus erythropolis WZ010 and its application for the synthesis of (2S,3S)-2,3-butanediol
Appl. Microbiol. Biotechnol.
98
641-650
2014
Rhodococcus erythropolis (C0ZPN9), Rhodococcus erythropolis PR4 (C0ZPN9)
brenda
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1.1.1.303 diacetyl reductase [(R)-acetoin forming]
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