Information on EC 1.1.1.B51 - 3-quinuclidinone reductase (NADPH)

for references in articles please use BRENDA:EC1.1.1.B51
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.1.1.B51
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
3-quinuclidinone reductase (NADPH)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(R)-3-quinuclidinol + NADP+ = 3-quinuclidinone + NADPH + H+
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
(R)-3-quinuclidinol:NADP+ oxidoreductase
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-quinuclidinone + NADPH + H+
(R)-3-quinuclidinol + NADP+
show the reaction diagram
ethyl 4-chloro-3-oxobutanoate + NADPH + H+
ethyl (S)-4-chloro-3-hydroxybutanoate + NADP+
show the reaction diagram
ketopantoyl lactone + NADPH + H+
pantoyl lactone + NADP+
show the reaction diagram
additional information
?
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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
3-quinuclidinone + NADPH + H+
(R)-3-quinuclidinol + NADP+
show the reaction diagram
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stereospecific reduction of 3-quinuclidinone
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-mercuribenzoate
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1 mM, complete inhibition
5,5'-dithiobis(2-nitrobenzoate)
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1 mM, 15% inhibition
Hg2+
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1 mM, complete inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1 - 145
3-quinuclidinone
0.19
NADPH
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pH 7.0, temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.69 - 15.1
3-quinuclidinone
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
341
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pH 7.0, temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
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apart from D-glucose and glycerol, various sugars and alcohols like maltose, sucrose, arabinose, mannitol, sorbitol are not utilized by strain WY1202 for growth
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
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3 or 4 * 3 * 30000, SDS-PAGE
93000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting-drop vapor-diffusion method with a reservoir solution containing 100 mM CHES (pH 10.0), 30% PEG8000, and 3% sucrose, at 5C
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sitting-drop vapour-diffusion method using PEG 8000 as the precipitant. The crystals belonged to space group P4(1)2(1)2, with unit-cell parameters a = b = 91.3, c = 265.4 A, and diffracted X-rays to 2.2 A resolution.The asymmetric unit contained four molecules of the protein and the solvent content was 48.4%
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-affinity and ion-exchange column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an expression vector, pWKLQ, which contains the full length 3-quinuclidinone reductase gene is constructed. Using Escherichia coli cells coexpressing the 3-quinuclidinone reductase and glucose dehydrogenase (cofactor regeneration enzyme) genes, 618 mM 3-quinuclidinone is almost stiochiometrically converted to (R)-3-quinuclidinol with an >99.9% enantiomeric excess within 21 h of reaction
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expressed in Escherichia coli
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phylogenetic tree
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F212A
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complete loss of activity
F212L
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complete loss of activity
I167A
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complete loss of activity
I167V
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relative activity for 3-qinuclidinone is 24.5% compared to wild-type enzyme
K185A
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complete loss of activity
N173A
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relative activity for 3-qinuclidinone is 97.8% compared to wild-type enzyme
Q178A
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relative activity for 3-qinuclidinone is 164.5% compared to wild-type enzyme
S166A
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complete loss of activity
S168A
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relative activity for 3-qinuclidinone is 115.7% compared to wild-type enzyme
Y181A
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complete loss of activity
Y181F
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complete loss of activity
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pharmacology
synthesis