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Information on EC 1.1.1.B52 - 3-quinuclidinone reductase (NADH)
for references in articles please use BRENDA:EC1.1.1.B52
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preliminary BRENDA-supplied EC number
EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.B52 3-quinuclidinone reductase (NADH)
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 1.1.1.B52
-
rhodotorula
- synthesis
- rubra
- pharmacology
- tumefaciens
-
agrobacterium
- peg
- nicotinamide
-
phosphate-dependent
-
protomer
-
nadh-dependent
-
vapour-diffusion
-
sitting-drop
showSynonyms
3-quinuclidinone reductase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BacC
QNR
BacC
bacC isolated from Microbacterium luteolum shows 99.9% identity (100% amino acid identity) with the putative oxidoreductase gene bacC of the bacilysin biosynthetic gene cluster derived from Bacillus subtilis, suggesting that bacC is horizontally transferred from Bacillus species
BacC
bacC isolated from Microbacterium luteolum shows 99.9% identity (100% amino acid identity) with the putative oxidoreductase gene bacC of the bacilysin biosynthetic gene cluster derived from Bacillus subtilis, suggesting that bacC is horizontally transferred from Bacillus species
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(R)-3-quinuclidinol + NAD+ = 3-quinuclidinone + NADH + H+
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
(R)-3-quinuclidinol:NAD+ oxidoreductase
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
Substrates: enzyme is an alcohol dehydrogenase, reaction of EC 1.1.1.1
Products: -
Products: -
?
2-acetylpyridine + NADH + H+
?
Substrates: activity is 16.8% compared to the activity with 3-quinuclidinone, 3-quinuclidinone reductase BacC
Products: -
Products: -
?
2-acetylpyridine + NADH + H+
?
Substrates: activity is 16.8% compared to the activity with 3-quinuclidinone, 3-quinuclidinone reductase BacC
Products: -
Products: -
?
3-quinuclidinone + NADH + H+
(R)-3-quinuclidinol + NAD+
Substrates: high activity and excellent enantioselectivity
Products: -
Products: -
?
3-quinuclidinone + NADH + H+
(R)-3-quinuclidinol + NAD+
Substrates: stereospecific reduction of 3-quinuclidinone
Products: -
Products: -
?
3-quinuclidinone + NADH + H+
(R)-3-quinuclidinol + NAD+
Substrates: under the optimized conditions, (R)-(-)-3-quinuclidinolis synthesized from 3-quinuclidinone (15% w/v, 939 mM) gives a conversion yield of 100% for the immobilized enzyme. The optical purity of the (R)-(-)-3-quinuclidinol produced by the enzymatic reactions is above 99.9%
Products: -
Products: -
?
3-quinuclidinone + NADH + H+
(R)-3-quinuclidinol + NAD+
Substrates: 3-quinuclidinone (5% w/v, 313 mM) is reduced to (R)-3-quinuclidinol with a molar conversion yield of 100% by 3-quinuclidinone reductase QNR. The optical purity is above 99.9%. No activity with NADPH. The enzyme is strictly specific for 3-quinuclidinone and shows no activity toward several ketones, including tropinone
Products: -
Products: -
?
3-quinuclidinone + NADH + H+
(R)-3-quinuclidinol + NAD+
Substrates: 3-quinuclidinone (5% w/v, 313 mM) is reduced to (R)-3-quinuclidinol with a molar conversion yield of 94% bei 3-quinuclidinone reductase BacC. The optical purity is above 99.9%. No activity with NADPH
Products: -
Products: -
?
3-quinuclidinone + NADH + H+
(R)-3-quinuclidinol + NAD+
Substrates: under the optimized conditions, (R)-(-)-3-quinuclidinolis synthesized from 3-quinuclidinone (15% w/v, 939 mM) gives a conversion yield of 100% for the immobilized enzyme. The optical purity of the (R)-(-)-3-quinuclidinol produced by the enzymatic reactions is above 99.9%
Products: -
Products: -
?
3-quinuclidinone + NADH + H+
(R)-3-quinuclidinol + NAD+
Substrates: 3-quinuclidinone (5% w/v, 313 mM) is reduced to (R)-3-quinuclidinol with a molar conversion yield of 100% by 3-quinuclidinone reductase QNR. The optical purity is above 99.9%. No activity with NADPH. The enzyme is strictly specific for 3-quinuclidinone and shows no activity toward several ketones, including tropinone
Products: -
Products: -
?
3-quinuclidinone + NADH + H+
(R)-3-quinuclidinol + NAD+
Substrates: 3-quinuclidinone (5% w/v, 313 mM) is reduced to (R)-3-quinuclidinol with a molar conversion yield of 94% bei 3-quinuclidinone reductase BacC. The optical purity is above 99.9%. No activity with NADPH
Products: -
Products: -
?
3-quinuclidinone + NADH + H+
(R)-3-quinuclidinol + NAD+
-
Substrates: -
Products: 84% ee, 62% conversion after 22 h
Products: 84% ee, 62% conversion after 22 h
?
7-oxabicyclo[4.1.0]heptan-2-one + NADH + H+
?
Substrates: activity is 27.8% compared to the activity with 3-quinuclidinone, 3-quinuclidinone reductase BacC
Products: -
Products: -
?
7-oxabicyclo[4.1.0]heptan-2-one + NADH + H+
?
Substrates: activity is 27.8% compared to the activity with 3-quinuclidinone, 3-quinuclidinone reductase BacC
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-quinuclidinone + NADH + H+
(R)-3-quinuclidinol + NAD+
Substrates: stereospecific reduction of 3-quinuclidinone
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
three NADH-bound protomers and one NADH-free protomer form a tetrameric structure in an asymmetric unit of crystals. NADH not only acts as a proton donor, but also contributes to the stability of the alpha7 helix. NADH is located in a deep cleft of the large domain and bound at the C-terminal end of the beta-sheet. The adenosine moiety of NADH is bound to a pocket formed by Gly16, Leu41, Val62, Asp63, Val64, Thr65, Ala91, Val93, and Val113. Residue Asp40 plays an important role in binding to NADH
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.4
3-quinuclidinone
pH 7.0, temperature not specified in the publication
6.5
3-quinuclidinone
pH 7.0, 25°C, 3-quinuclidinone reductase QNR
13.8
3-quinuclidinone
pH 7.0, 25°C, 3-quinuclidinone reductase BacC
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
290
3-quinuclidinone
pH 7.0, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
AtQR has all three catalytic residues of the short-chain dehydrogenases/reductases family and the hydrophobic wall for the enantioselective reduction of 3-quinuclidinone
additional information
additional information
the alpha7 helix is a unique and functionally significant part of AtQR and is related to form a deep catalytic cavity, it is stabilized by NADH. An additional residue on the a7 helix, Glu197, exists near the active site of AtQR. This acidic residue is considered to form a direct interaction with the amine part of 3-quinuclidinone, which contributes to substrate orientation and enhancement of substrate-binding affinity. Glu197 is an indispensable residue for the enzyme activity. Asp40 plays an important role in binding to NADH. Glu197 may be the key residue for enhancing the substrate-binding affinity. Structure-function anaysis and enantioselectivity, overview.
additional information
-
the alpha7 helix is a unique and functionally significant part of AtQR and is related to form a deep catalytic cavity, it is stabilized by NADH. An additional residue on the a7 helix, Glu197, exists near the active site of AtQR. This acidic residue is considered to form a direct interaction with the amine part of 3-quinuclidinone, which contributes to substrate orientation and enhancement of substrate-binding affinity. Glu197 is an indispensable residue for the enzyme activity. Asp40 plays an important role in binding to NADH. Glu197 may be the key residue for enhancing the substrate-binding affinity. Structure-function anaysis and enantioselectivity, overview.
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). G1K3P5_AGRTU
263
0
27562
TrEMBL
other Location (Reliability: 3)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
tetramer
three NADH-bound protomers and one NADH-free protomer form a tetrameric structure in an asymmetric unit of crystals, quaternary structure of AtQR, overview
trimer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged enzyme, enzyme AtQR and 2 mM NADH are crystallized from a reservoir solution containing of 0.2 M ammonium acetate, 0.1 M HEPES, pH 8.5, and 24% w/v PEG 3350, X-ray diffraction structure determination and analysis at 1.72 A resolution. Three NADH-bound protomers and one NADH-free protomer form a tetrameric structure in an asymmetric unit of crystals. NADH not only acts as a proton donor, but also contributes to the stability of the alpha7 helix. Molecular replacement using structure of meso-2,3-butanediol dehydrogenase, PDB ID 1GEG, from Klebsiella pneumoniae as template
sitting-drop vapour-diffusion method at 20°C. 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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R196A
site-directed mutagenesis, the mutant shows 34% reduced activity compared to the wild-type enzyme
Y216V
site-directed mutagenesis, the mutant shows 69% reduced activity compared to the wild-type enzyme
A158A/N162P
-
96.8% enantiomeric excess for (R)-3-quinuclidinol production, 82% conversion
A158D/N162G
-
96.5% enantiomeric excess for (R)-3-quinuclidinol production, 87% conversion
A158D/N162Q
-
95.8% enantiomeric excess for (R)-3-quinuclidinol production, 79% conversion
A158H/N162G/K202Q/L224W
-
mutations increase the enantiomeric excess for (R)-3-quinuclidinol production from 84.3% (wild-type) to 99% and concomitantly to enhance conversion by 43.5%
A158H/N162P
-
98.1% enantiomeric excess for (R)-3-quinuclidinol production, 95% conversion
A158K/N162M
-
97.6% enantiomeric excess for (R)-3-quinuclidinol production, 98% conversion
K202N/L224M
-
89.7% enantiomeric excess for (R)-3-quinuclidinol production, 90% conversion
K202Q/L224W
-
95.5% enantiomeric excess for (R)-3-quinuclidinol production, 82% conversion
K202R/L224W
-
94.7% enantiomeric excess for (R)-3-quinuclidinol production, 91% conversion
K202S/L224Y
-
89.5% enantiomeric excess for (R)-3-quinuclidinol production, 82% conversion
N162A
-
93.8% enantiomeric excess for (R)-3-quinuclidinol production, 91% conversion
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminally His6-tagged enzyme from Eschrichia coli strain Rosetta(DE3) by nickel affinity and anion exchange chromatography, and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
recombinant expression of N-terminally His6-tagged enzyme in Eschrichia coli strain Rosetta(DE3)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pharmacology
synthesis
pharmacology
stereospecific production of (R)-3-quinuclidinol, an important chiral building block for the synthesis of various pharmaceuticals. The 3-quinuclidinone reductase and Leifsonia sp. alcohol dehydrogenase genes are efficiently expressed in Escherichia coli cells. A number of constructed Echerichia coli biocatalysts (intact or immobilized) are applied to the resting cell reaction and optimized. Under the optimized conditions, (R)-(-)-3-quinuclidinolis synthesized from 3-quinuclidinone (15% w/v, 939 mM) giving a conversion yield of 100% for the immobilized enzyme. The optical purity of the (R)-(-)-3-quinuclidinol produced by the enzymatic reactions is above 99.9%
pharmacology
stereospecific production of (R)-3-quinuclidinol, an important chiral building block for the synthesis of various pharmaceuticals
pharmacology
stereospecific production of (R)-3-quinuclidinol, an important chiral building block for the synthesis of various pharmaceuticals, high yield of (R)-3-quinuclidinol up to 916 g/L * d using a bioreduction approach
pharmacology
-
stereospecific production of (R)-3-quinuclidinol, an important chiral building block for the synthesis of various pharmaceuticals. The 3-quinuclidinone reductase and Leifsonia sp. alcohol dehydrogenase genes are efficiently expressed in Escherichia coli cells. A number of constructed Echerichia coli biocatalysts (intact or immobilized) are applied to the resting cell reaction and optimized. Under the optimized conditions, (R)-(-)-3-quinuclidinolis synthesized from 3-quinuclidinone (15% w/v, 939 mM) giving a conversion yield of 100% for the immobilized enzyme. The optical purity of the (R)-(-)-3-quinuclidinol produced by the enzymatic reactions is above 99.9%
-
pharmacology
-
stereospecific production of (R)-3-quinuclidinol, an important chiral building block for the synthesis of various pharmaceuticals
-
synthesis
stereospecific production of (R)-3-quinuclidinol, an important chiral building block for the synthesis of various pharmaceuticals. The 3-quinuclidinone reductase and Leifsonia sp. alcohol dehydrogenase genes are efficiently expressed in Escherichia coli cells. A number of constructed Echerichia coli biocatalysts (intact or immobilized) are applied to the resting cell reaction and optimized. Under the optimized conditions, (R)-(-)-3-quinuclidinolis synthesized from 3-quinuclidinone (15% w/v, 939 mM) giving a conversion yield of 100% for the immobilized enzyme. The optical purity of the (R)-(-)-3-quinuclidinol produced by the enzymatic reactions is above 99.9%
synthesis
stereospecific production of (R)-3-quinuclidinol, an important chiral building block for the synthesis of various pharmaceuticals
synthesis
stereospecific production of (R)-3-quinuclidinol, an important chiral building block for the synthesis of various pharmaceuticals, high yield of (R)-3-quinuclidinol up to 916 g/L * d using a bioreduction approach
synthesis
-
stereospecific production of (R)-3-quinuclidinol, an important chiral building block for the synthesis of various pharmaceuticals. The 3-quinuclidinone reductase and Leifsonia sp. alcohol dehydrogenase genes are efficiently expressed in Escherichia coli cells. A number of constructed Echerichia coli biocatalysts (intact or immobilized) are applied to the resting cell reaction and optimized. Under the optimized conditions, (R)-(-)-3-quinuclidinolis synthesized from 3-quinuclidinone (15% w/v, 939 mM) giving a conversion yield of 100% for the immobilized enzyme. The optical purity of the (R)-(-)-3-quinuclidinol produced by the enzymatic reactions is above 99.9%
-
synthesis
-
stereospecific production of (R)-3-quinuclidinol, an important chiral building block for the synthesis of various pharmaceuticals
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hou, F.; Miyakawa, T.; Takeshita, D.; Kataoka, M.; Uzura, A.; Nagata, K.; Shimizu, S.; Tanokura, M.
Expression, purification, crystallization and X-ray analysis of 3-quinuclidinone reductase from Agrobacterium tumefaciens
Acta Crystallogr. Sect. F
68
1237-1239
2012
Agrobacterium tumefaciens (G1K3P5), Agrobacterium tumefaciens
brenda
Isotani, K.; Kurokawa, J.; Suzuki, F.; Nomoto, S.; Negishi, T.; Matsuda, M.; Itoh, N.
Gene cloning and characterization of two NADH-dependent 3-quinuclidinone reductases from Microbacterium luteolum JCM 9174
Appl. Environ. Microbiol.
79
1378-1384
2012
Microbacterium luteolum (L8B2H6), Microbacterium luteolum JCM 9174 (L8B2H6)
brenda
Isotani, K.; Kurokawa, J.; Itoh, N.
Production of (R)-3-quinuclidinol by E. coli biocatalysts possessing NADH-dependent 3-quinuclidinone reductase (QNR or bacC) from Microbacterium luteolum and Leifsonia alcohol dehydrogenase (LSADH)
Int. J. Mol. Sci.
13
13542-13553
2012
Microbacterium luteolum (L8B2H6), Microbacterium luteolum, Microbacterium luteolum JCM 9174 (L8B2H6)
brenda
Zhang, W.X.; Xu, G.C.; Huang, L.; Pan, J.; Yu, H.L.; Xu, J.H.
Highly efficient synthesis of (R)-3-quinuclidinol in a space-time yield of 916 g L(-1) d(-1) using a new bacterial reductase ArQR
Org. Lett.
15
4917-4919
2013
Agrobacterium tumefaciens (G1K3P5)
brenda
Spickermann, D.; Hausmann, S.; Degering, C.; Schwaneberg, U.; Leggewie, C.
Engineering of highly selective variants of Parvibaculum lavamentivorans alcohol dehydrogenase
ChemBioChem
15
2050-2052
2014
Parvibaculum lavamentivorans
brenda
Hou, F.; Miyakawa, T.; Kataoka, M.; Takeshita, D.; Kumashiro, S.; Uzura, A.; Urano, N.; Nagata, K.; Shimizu, S.; Tanokura, M.
Structural basis for high substrate-binding affinity and enantioselectivity of 3-quinuclidinone reductase AtQR
Biochem. Biophys. Res. Commun.
446
911-915
2014
Agrobacterium tumefaciens (G1K3P5), Agrobacterium tumefaciens
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.B52)
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