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Information on EC 1.1.1.304 - diacetyl reductase [(S)-acetoin forming] and Organism(s) Klebsiella pneumoniae and UniProt Accession Q48436

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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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This record set is specific for:
Klebsiella pneumoniae
UNIPROT: Q48436
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The taxonomic range for the selected organisms is: Klebsiella pneumoniae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
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(S)-acetoin
+
NAD+
=
diacetyl
+
NADH
+
H+
+
=
+
+
Synonyms
diacetyl reductase, ppdar, ardii, readr, more
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].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,3-pentanedione + NADH + H+
3-hydroxy-2-pentanone + NAD+
show the reaction diagram
77% of the (R)-2,3-butanediol dehydrogenase activity with substrate acetoin
-
-
?
diacetyl + NADH + H+
(S)-acetoin + NAD+
show the reaction diagram
diacetyl + NADH + H+
(S)-acetoin + NAD+
show the reaction diagram
-
-
-
r
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
diacetyl + NADH + H+
(S)-acetoin + NAD+
show the reaction diagram
-
-
-
?
diacetyl + NADH + H+
(S)-acetoin + NAD+
show the reaction diagram
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
79
pH 6.5, temperature not specified in the publication, with FDH
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.9 - 7.2
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
BUDC_KLEPN
256
0
26642
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26591
4 * 26591, calculated
96000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
4 * 26591, calculated
?
x * 28000, recombinant His-tagged enzyme, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8
-
704903
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene budC, functional recombinant expression of NADH-dependent Kp-BudC from plasmid pKM3 in Escherichia coli wild-type strain BW25113 and in mutant strain JCL166 (BW25113/F' [traD36, proABþ, lacIqZ DELTAM15 (Tet)] JCL16 DELTAadhE DELTAldhA DELTAfrdBC)
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha, coexpression with formate dehydrogenase (FDH) gene fdh from Saccharomyces cerevisiae or glucose dehydrogenase (GDH) gene gdh from Bacillus subtilis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ui, S.; Okajima, Y.; Mimura, A.; Kanai, H.; kobayashi, T.; Kudo, T.
Sequence analysis of the gene for and characterization of D-acetoin forming meso-2,3-butanediol dehydrogenase of Klebsiella pneumoniae expressed in Escherichia coli
J. Ferment. Bioeng.
83
32-37
1997
Klebsiella pneumoniae (Q48436)
-
Manually annotated by BRENDA team
Liang, K.; Shen, C.
Selection of an endogenous 2,3-butanediol pathway in Escherichia coli by fermentative redox balance
Metab. Eng.
39
181-191
2017
Klebsiella pneumoniae (Q48436)
Manually annotated by BRENDA team
Li, J.; Huang, Y.; Chen, X.; Du, Q.; Meng, J.; Xie, N.; Huang, R.
Enhanced production of optical (S)-acetoin by a recombinant Escherichia coli whole-cell biocatalyst with NADH regeneration
RSC Adv.
8
30512-30519
2018
Klebsiella pneumoniae (D7RP28), Mycobacterium sp. B-009 (W8VSK8), Paenibacillus polymyxa (A0A5B8J1I7), Rhodococcus erythropolis (M4N626), Rhodococcus erythropolis WZ010 (M4N626)
-
Manually annotated by BRENDA team