Information on EC 1.1.1.B52 - 3-quinuclidinone reductase (NADH)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.1.B52
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
3-quinuclidinone reductase (NADH)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(R)-3-quinuclidinol + NAD+ = 3-quinuclidinone + NADH + H+
show the reaction diagram
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-
-
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SYSTEMATIC NAME
IUBMB Comments
(R)-3-quinuclidinol:NAD+ oxidoreductase
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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
2-acetylpyridine + NADH + H+
?
show the reaction diagram
3-quinuclidinone + NADH + H+
(R)-3-quinuclidinol + NAD+
show the reaction diagram
7-oxabicyclo[4.1.0]heptan-2-one + NADH + H+
?
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.4 - 13.8
3-quinuclidinone
0.02 - 0.03
NADH
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
290
3-quinuclidinone
Agrobacterium tumefaciens
B9JM87
pH 7.0, temperature not specified in the publication
48633
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.5
-
pH 7.0, 25C, 3-quinuclidinone reductase BacC
8.4
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pH 7.0, 25C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8
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3-quinuclidinone reductase QNR
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
72000
-
gel filtration, 3-quinuclidinone reductase BacC
94000
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gel filtration, 3-quinuclidinone reductase QNR
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trimer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystallized under a reservoir solution condition of 0.2 M ammonium acetate, 0.1 M HEPES pH 8.5 and 24% (w/v) PEG3350
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sitting-drop vapour-diffusion method at 20C. Crystals are obtained using a reservoir solution containing PEG 3350 as a precipitant. X-ray diffraction data are collected to 1.72 A resolution. The crystal belongs to space group P2(1), with unit-cell parameters a = 62.0, b = 126.4, c = 62.0 A, beta = 110.5, and is suggested to contain four molecules in the asymmetric unit
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
NADH contributes to the stability of the alpha7 helix of the enzyme
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; 3-quinuclidinone reductase QNR
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli. The gene is fused with the His6 tag and thrombin recognition sequence at the N-terminus under the control of the T7 promoter, 3-quinuclidinone reductase BacC; expression in Escherichia coli. The gene is fused with the His6 tag and thrombin recognition sequence at the N-terminus under the control of the T7 promoter, 3-quinuclidinone reductase QNR
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overexpressed as a fusion protein with an N-terminal His6 tag in Eschrichia coli Rosetta(DE3)
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overexpressed in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D40A
-
no activity
E197A
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no activity
R196A
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activity is 76% compared to activity of wild-type enzyme
Y216V
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activity is 31% compared to activity of wild-type enzyme
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pharmacology
synthesis