1.1.1.B52: 3-quinuclidinone reductase (NADH)
This is an abbreviated version!
For detailed information about 3-quinuclidinone reductase (NADH), go to the full flat file.
Word Map on EC 1.1.1.B52
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1.1.1.B52
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rhodotorula
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synthesis
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rubra
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pharmacology
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tumefaciens
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agrobacterium
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peg
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nicotinamide
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phosphate-dependent
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protomer
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nadh-dependent
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vapour-diffusion
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sitting-drop
- 1.1.1.B52
-
rhodotorula
- synthesis
- rubra
- pharmacology
- tumefaciens
-
agrobacterium
- peg
- nicotinamide
-
phosphate-dependent
-
protomer
-
nadh-dependent
-
vapour-diffusion
-
sitting-drop
Reaction
Synonyms
3-quinuclidinone reductase, alcohol dehydrogenase, ArQR, AtQR, BacC, NADHdependent 3-quinuclidionone reductase, QNR
ECTree
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Engineering
Engineering on EC 1.1.1.B52 - 3-quinuclidinone reductase (NADH)
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D40A
E197A
R196A
Y216V
A158A/N162P
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96.8% enantiomeric excess for (R)-3-quinuclidinol production, 82% conversion
A158D/N162G
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96.5% enantiomeric excess for (R)-3-quinuclidinol production, 87% conversion
A158D/N162Q
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95.8% enantiomeric excess for (R)-3-quinuclidinol production, 79% conversion
A158H/N162G/K202Q/L224W
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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
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98.1% enantiomeric excess for (R)-3-quinuclidinol production, 95% conversion
A158K/N162M
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97.6% enantiomeric excess for (R)-3-quinuclidinol production, 98% conversion
K202N/L224M
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89.7% enantiomeric excess for (R)-3-quinuclidinol production, 90% conversion
K202Q/L224W
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95.5% enantiomeric excess for (R)-3-quinuclidinol production, 82% conversion
K202R/L224W
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94.7% enantiomeric excess for (R)-3-quinuclidinol production, 91% conversion
K202S/L224Y
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89.5% enantiomeric excess for (R)-3-quinuclidinol production, 82% conversion
N162A
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93.8% enantiomeric excess for (R)-3-quinuclidinol production, 91% conversion
site-directed mutagenesis, the mutant shows 34% reduced activity compared to the wild-type enzyme
R196A
activity is 76% compared to activity of wild-type enzyme
activity is 31% compared to activity of wild-type enzyme
Y216V
site-directed mutagenesis, the mutant shows 69% reduced activity compared to the wild-type enzyme