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2-acetylpyridine + NADH + H+
?
2-acetylpyridine + NADH + H+
? + NAD+
3-quinuclidinone + NADH + H+
(R)-3-quinuclidinol + NAD+
7-oxabicyclo[4.1.0]heptan-2-one + NADH + H+
?
7-oxabicyclo[4.1.0]heptan-2-one + NADH + H+
? + NAD+
Substrates: 27.8% of the activity with 3-quinuclidinone
Products: -
?
additional information
?
-
2-acetylpyridine + NADH + H+
?
Substrates: activity is 16.8% compared to the activity with 3-quinuclidinone, 3-quinuclidinone reductase BacC
Products: -
?
2-acetylpyridine + NADH + H+
?
Substrates: activity is 16.8% compared to the activity with 3-quinuclidinone, 3-quinuclidinone reductase BacC
Products: -
?
2-acetylpyridine + NADH + H+
? + NAD+
Substrates: 16.8% of the activity with 3-quinuclidinone
Products: -
?
2-acetylpyridine + NADH + H+
? + NAD+
Substrates: 16.8% of the activity with 3-quinuclidinone
Products: -
?
3-quinuclidinone + NADH + H+
(R)-3-quinuclidinol + NAD+
Substrates: high activity and excellent enantioselectivity
Products: -
?
3-quinuclidinone + NADH + H+
(R)-3-quinuclidinol + NAD+
Substrates: stereospecific reduction of 3-quinuclidinone
Products: -
?
3-quinuclidinone + NADH + H+
(R)-3-quinuclidinol + NAD+
Substrates: -
Products: -
ir
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: -
?
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: -
?
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: -
?
3-quinuclidinone + NADH + H+
(R)-3-quinuclidinol + NAD+
Substrates: over 99.9% enantiomeric excess
Products: -
ir
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: -
?
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: -
?
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: -
?
3-quinuclidinone + NADH + H+
(R)-3-quinuclidinol + NAD+
Substrates: -
Products: -
ir
3-quinuclidinone + NADH + H+
(R)-3-quinuclidinol + NAD+
Substrates: over 99.9% enantiomeric excess
Products: -
ir
3-quinuclidinone + NADH + H+
(R)-3-quinuclidinol + NAD+
-
Substrates: -
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: -
?
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: -
?
additional information
?
-
Substrates: the enzyme shows narrow substrate specificity and high stereoselectivity for the reduction of 3-quinuclidinone to (R)-3-quinuclidinol. No activity with (R)-3-quinuclidinol, 2-acetylpyridine, and 7-oxabicyclo[4.1.0]heptan-2-one, as well as with 2-propanol, acetone, acetophenone, 2,2,2-trifluoroacetophenone, 3-methylene-2-norbornanone, ethyl pyruvate, ethyl acetoacetate, 4-hydroxy-1-cyclohexanecarboxylic acid delta-lactone, verbenone, tropinone, 6-hydroxytropinone, 2-azabicyclo[2,2,1]hept-5-en-3-one, 1-methyl-4-piperidone, 3-acetylpyridine, 4-acetylpyridine, cyclohexanone, 2-methylcyclohexanone, 3-methylcyclohexanone, and tetrahydrothiopyran-4-one
Products: -
?
additional information
?
-
Substrates: the enzyme shows narrow substrate specificity and high stereoselectivity for the reduction of 3-quinuclidinone to (R)-3-quinuclidinol. No activity with (R)-3-quinuclidinol, 2-propanol, acetone, acetophenone, 2,2,2-trifluoroacetophenone, 3-methylene-2-norbornanone, ethyl pyruvate, ethyl acetoacetate, 4-hydroxy-1-cyclohexanecarboxylic acid delta-lactone, verbenone, tropinone, 6-hydroxytropinone, 2-azabicyclo[2,2,1]hept-5-en-3-one, 1-methyl-4-piperidone, 3-acetylpyridine, 4-acetylpyridine, cyclohexanone, 2-methylcyclohexanone, 3-methylcyclohexanone, and tetrahydrothiopyran-4-one
Products: -
?
additional information
?
-
Substrates: the enzyme shows narrow substrate specificity and high stereoselectivity for the reduction of 3-quinuclidinone to (R)-3-quinuclidinol. No activity with (R)-3-quinuclidinol, 2-acetylpyridine, and 7-oxabicyclo[4.1.0]heptan-2-one, as well as with 2-propanol, acetone, acetophenone, 2,2,2-trifluoroacetophenone, 3-methylene-2-norbornanone, ethyl pyruvate, ethyl acetoacetate, 4-hydroxy-1-cyclohexanecarboxylic acid delta-lactone, verbenone, tropinone, 6-hydroxytropinone, 2-azabicyclo[2,2,1]hept-5-en-3-one, 1-methyl-4-piperidone, 3-acetylpyridine, 4-acetylpyridine, cyclohexanone, 2-methylcyclohexanone, 3-methylcyclohexanone, and tetrahydrothiopyran-4-one
Products: -
?
additional information
?
-
Substrates: the enzyme shows narrow substrate specificity and high stereoselectivity for the reduction of 3-quinuclidinone to (R)-3-quinuclidinol. No activity with (R)-3-quinuclidinol, 2-propanol, acetone, acetophenone, 2,2,2-trifluoroacetophenone, 3-methylene-2-norbornanone, ethyl pyruvate, ethyl acetoacetate, 4-hydroxy-1-cyclohexanecarboxylic acid delta-lactone, verbenone, tropinone, 6-hydroxytropinone, 2-azabicyclo[2,2,1]hept-5-en-3-one, 1-methyl-4-piperidone, 3-acetylpyridine, 4-acetylpyridine, cyclohexanone, 2-methylcyclohexanone, 3-methylcyclohexanone, and tetrahydrothiopyran-4-one
Products: -
?
additional information
?
-
-
Substrates: enzyme is an alcohol dehydrogenase, reaction of EC 1.1.1.1
Products: -
?
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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
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
-
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%
-
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
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
(R)-3-quinuclidinol is a valuable intermediate for pharmaceuticals. The enzyme can be used for the synthesis of the enantiopure compound
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. 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
-
(R)-3-quinuclidinol is a valuable intermediate for pharmaceuticals. The enzyme can be used for the synthesis of the enantiopure compound
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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
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
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
2013
Microbacterium luteolum (L8B2H6), Microbacterium luteolum JCM 9174 (L8B2H6)
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