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

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EC NUMBER
COMMENTARY hide
1.1.1.303
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RECOMMENDED NAME
GeneOntology No.
diacetyl reductase [(R)-acetoin forming]
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(R)-acetoin + NAD+ = diacetyl + NADH + H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
pyruvate fermentation to (R)-acetoin I
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acetoin degradation
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Butanoate metabolism
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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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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene adr
UniProt
Manually annotated by BRENDA team
gene adr
UniProt
Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
physiological function
gene disruption is not lethal. Disrupted strains can grow on 2,3-butanediol, but to a lesser cell density than wild-type
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,2-cyclohexanedione + NADH + H+
(R)-2-hydroxy-1-cyclohexanone + NAD+
show the reaction diagram
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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+
show the reaction diagram
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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+
show the reaction diagram
additional information
?
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enzyme is specific for NADH
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
diacetyl + NADH + H+
(R)-acetoin + NAD+
show the reaction diagram
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
Michaelis-Menten-type kinetics
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35000
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4 * 35000, SDS-PAGE
140000
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gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
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4 * 35000, SDS-PAGE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene adr, DNA and amino acid sequence determination and analysis, sequence comparison
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Show AA Sequence (168 entries)
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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.303)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)