1.14.13.16: cyclopentanone monooxygenase
This is an abbreviated version!
For detailed information about cyclopentanone monooxygenase, go to the full flat file.
Word Map on EC 1.14.13.16
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1.14.13.16
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baeyer-villiger
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biooxidation
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lactones
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polyelectrolyte
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encapsulated
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enantioselective
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capsules
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flavin
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cyclohexanone
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cellulose
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synthesis
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alginate
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enantiomeric
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regioisomeric
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conversions
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propidium
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immobilised
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polyvinyl
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autofluorescence
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biocatalysis
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ketone
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ncimb
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iodide
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regio
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halved
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drug development
- 1.14.13.16
-
baeyer-villiger
-
biooxidation
- lactones
-
polyelectrolyte
-
encapsulated
-
enantioselective
- capsules
- flavin
- cyclohexanone
- cellulose
- synthesis
- alginate
-
enantiomeric
-
regioisomeric
-
conversions
- propidium
-
immobilised
-
polyvinyl
-
autofluorescence
-
biocatalysis
- ketone
-
ncimb
- iodide
-
regio
-
halved
- drug development
Reaction
Synonyms
CPMO, CpnB, cyclopentanone monooxygenase, cyclopentanone oxygenase, More
ECTree
1.14.13.16 cyclopentanone monooxygenaseAdvanced search results
results (
results (Results
in table
15
19
24
15
Engineering
Engineering on EC 1.14.13.16 - cyclopentanone monooxygenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
F156H/G157L
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site-directed mutagenesis, the mutant shows altered substrate specificity and stereoselectivity compared to the wild-type enzyme
F156L/G157F
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site-directed mutagenesis, the mutations improve the hydrophobic active site pocket increasing enzyme selectivity and stereospecificity
F156N/G157Y
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site-directed mutagenesis, the mutant shows altered substrate specificity and stereoselectivity compared to the wild-type enzyme
F450C
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site-directed mutagenesis, the mutant shows altered substrate specificity and stereoselectivity compared to the wild-type enzyme
F450I
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site-directed mutagenesis, the mutant shows altered substrate specificity and stereoselectivity compared to the wild-type enzyme
G119S/F450Y
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site-directed mutagenesis, the mutant shows altered substrate specificity and stereoselectivity compared to the wild-type enzyme
F156N/G157Y
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site-directed mutagenesis, the mutant shows altered substrate specificity and stereoselectivity compared to the wild-type enzyme
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F450C
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site-directed mutagenesis, the mutant shows altered substrate specificity and stereoselectivity compared to the wild-type enzyme
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F450I
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site-directed mutagenesis, the mutant shows altered substrate specificity and stereoselectivity compared to the wild-type enzyme
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G119S/F450Y
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site-directed mutagenesis, the mutant shows altered substrate specificity and stereoselectivity compared to the wild-type enzyme
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additional information
additional information
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active site mutations to improve enantioselectivity of the enzyme towards 4-substituted cyclohexanone substrates, method evaluation, overview, the effect of mutation of residues 449 and 450 does not have a full impact on the improvement of the hydrophobic pocket
additional information
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mutations in the active site residues responsible for stereoselectivity is a shortcut to an improvement in enantioselectivity in the often unselective CPMO, the combination of rational design and random mutagenesis at the predefined positions gives rise to focused libraries for improvement of the catalytic performance of enzymes, including enhanced enantioselectivity, using Complete Active Site Saturation Test, CAST, overview
additional information
-
mutations in the active site residues responsible for stereoselectivity is a shortcut to an improvement in enantioselectivity in the often unselective CPMO, the combination of rational design and random mutagenesis at the predefined positions gives rise to focused libraries for improvement of the catalytic performance of enzymes, including enhanced enantioselectivity, using Complete Active Site Saturation Test, CAST, overview
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additional information
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active site mutations to improve enantioselectivity of the enzyme towards 4-substituted cyclohexanone substrates, method evaluation, overview, the effect of mutation of residues 449 and 450 does not have a full impact on the improvement of the hydrophobic pocket
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additional information
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completion of the formal total synthesis of (+)-showdomycin and establishing of the absolute configuration of biooxidation product as (1S,6S)-3,9-dioxabicyclo[4.2.1]non-7-en-4-one, overview
