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

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The expected taxonomic range for this enzyme is: Rhodotorula mucilaginosa

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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-
-
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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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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
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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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