1.4.3.12: cyclohexylamine oxidase
This is an abbreviated version!
For detailed information about cyclohexylamine oxidase, go to the full flat file.
Word Map on EC 1.4.3.12
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1.4.3.12
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brevibacterium
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deracemization
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oxydans
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monoamine
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alicyclic
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cyclohexanone
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biocatalytic
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deamination
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flavin
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monooxygenase
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stereoselective
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cage
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flavoprotein
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enantiomeric
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dextromethorphan
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fad
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prosthetic
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racemic
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oxidases
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chaas
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synthesis
- 1.4.3.12
- brevibacterium
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deracemization
- oxydans
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monoamine
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alicyclic
- cyclohexanone
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biocatalytic
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deamination
- flavin
- monooxygenase
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stereoselective
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cage
- flavoprotein
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enantiomeric
- dextromethorphan
- fad
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prosthetic
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racemic
- oxidases
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chaas
- synthesis
Reaction
Synonyms
ArCHAO, CF596_10820, chaA, CHAO, CHAOCCH12-C2
ECTree
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Engineering
Engineering on EC 1.4.3.12 - cyclohexylamine oxidase
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F317A
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kcat/Km for 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline is 30% of the wild-type value
F327A
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kcat/Km for 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline is 179% of the wild-type value
G202A
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kcat/Km for 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline is 298% of the wild-type value
I173A
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kcat/Km for 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline is 67% of the wild-type value
I201A
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kcat/Km for 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline is 24% of the wild-type value
L200A
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kcat/Km for 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline is 150% of the wild-type value
L295A
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kcat/Km for 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline is 30% of the wild-type value
L295I
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kcat/Km for 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline is 73% of the wild-type value
P396A
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kcat/Km for 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline is 1177% of the wild-type value
T203A
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kcat/Km for 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline is 63% of the wild-type value
F317A
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kcat/Km for 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline is 30% of the wild-type value
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G202A
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kcat/Km for 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline is 298% of the wild-type value
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I201A
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kcat/Km for 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline is 24% of the wild-type value
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L200A
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kcat/Km for 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline is 150% of the wild-type value
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T203A
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kcat/Km for 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline is 63% of the wild-type value
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L199A
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the mutant shows generally lower activity (decrease of 15-97%) towards most substrates compared to wild type enzyme with the exception of the larger substrates, such as cyclooctanamine and bicyclic (S)-1-aminotetraline
L199F
L199I
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the mutant is more active than the wild type enzyme toward the primary amines
L199T
L353M
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the mutant shows 7-445% higher activity towards primary aliphatic amines with cycloalkane or aromatic moieties
M226A
M226F
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the mutant shows reduced catalytic efficiency with (S)-1-phenylethanamine and increased catalytic efficiency with 2-methyl-1,2,3,4-tetrahydroquinoline compared to the wild type enzyme
M226I
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the mutant is more active than the wild type enzyme toward the primary amines
M226T
T198A
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the mutant exhibits enhanced activity relative to the wild type enzyme for most (S)-enantiomers of primary amines and some secondary amines
T198F
T198F/L199S
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the mutant exhibits 240times higher catalytic efficiency with 2-methyl-1,2,3,4-tetrahydroquinoline than the wild type enzyme. The mutant shows reduced catalytic efficiency with (S)-1-phenylethanamine compared to the wild type enzyme
T198F/L199S/M226F
T198I
Y321A
Y321F
Y321I
Y321I/ M226T
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29.8fold increase of kcat/Km for the substrate L-valine ethyl ester as compared to wild-type enzyme. Chemoenzymatic deracemization is applied to prepare D-valine from racemic valine ethyl ester or L-valine ethyl ester in high yield (up to 95%) with excellent optical purity (more than 99% enantiomeric excess) by employing cyclohexylamine oxidase (CHAO) variant Y321I/M226T exhibiting catalytic efficiency that is 30 times higher than that of the wild type enzyme
Y321I/M226T
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the double mutant acts on (S)-N-(prop-2-yn-1-yl)-2,3-dihydro-1H-inden-1-amine
Y321I/M226T/T198I
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15.1fold increase of kcat/Km for the substrate L-valine ethyl ester as compared to wild-type enzyme
Y321I/M226T/T198I/F199F
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7.5fold increase of kcat/Km for the substrate L-valine ethyl ester as compared to wild-type enzyme
Y321I/T198I
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14.2fold increase of kcat/Km for the substrate L-valine ethyl ester as compared to wild-type enzyme
Y321T
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the mutation enhances the enzyme activity toward the secondary amines
Y459T
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the mutant shows reduced catalytic efficiency with (S)-1-phenylethanamine and increased catalytic efficiency with 2-methyl-1,2,3,4-tetrahydroquinoline compared to the wild type enzyme
L199A
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the mutant shows generally lower activity (decrease of 15-97%) towards most substrates compared to wild type enzyme with the exception of the larger substrates, such as cyclooctanamine and bicyclic (S)-1-aminotetraline
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L199F
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2.1fold increase of kcat/Km for the substrate L-valine ethyl ester as compared to wild-type enzyme
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L199T
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the mutant shows reduced catalytic efficiency with (S)-1-phenylethanamine and increased catalytic efficiency with 2-methyl-1,2,3,4-tetrahydroquinoline compared to the wild type enzyme
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L353M
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the mutant shows 7-445% higher activity towards primary aliphatic amines with cycloalkane or aromatic moieties
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M226A
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the mutant displays an enhanced activity (5-400%) towards most substrates
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M226F
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the mutant shows reduced catalytic efficiency with (S)-1-phenylethanamine and increased catalytic efficiency with 2-methyl-1,2,3,4-tetrahydroquinoline compared to the wild type enzyme
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M226T
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1.3fold increase of kcat/Km for the substrate L-valine ethyl ester as compared to wild-type enzyme
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T198F
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the mutant shows reduced catalytic efficiency with (S)-1-phenylethanamine and increased catalytic efficiency with 2-methyl-1,2,3,4-tetrahydroquinoline compared to the wild type enzyme
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T198F/L199S
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the mutant exhibits 240times higher catalytic efficiency with 2-methyl-1,2,3,4-tetrahydroquinoline than the wild type enzyme. The mutant shows reduced catalytic efficiency with (S)-1-phenylethanamine compared to the wild type enzyme
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T198F/L199S/M226F
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the mutant exhibits 406times higher catalytic efficiency with 2-methyl-1,2,3,4-tetrahydroquinoline than the wild type enzyme. The mutant shows reduced catalytic efficiency with (S)-1-phenylethanamine compared to the wild type enzyme
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T198I
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2.55fold increase of kcat/Km for the substrate L-valine ethyl ester as compared to wild-type enzyme
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Y321A
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the mutant shows higher catalytic efficiency towards cyclooctanamine compared to the wild type enzyme
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Y321F
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the mutant shows higher catalytic efficiency towards cyclooctanamine compared to the wild type enzyme
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Y321I
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13fold increase of kcat/Km for the substrate L-valine ethyl ester as compared to wild-type enzyme
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Y321I/T198I
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14.2fold increase of kcat/Km for the substrate L-valine ethyl ester as compared to wild-type enzyme
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the mutant is more active than the wild type enzyme toward the primary amines
L199F
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2.1fold increase of kcat/Km for the substrate L-valine ethyl ester as compared to wild-type enzyme
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the mutant shows reduced catalytic efficiency with (S)-1-phenylethanamine and increased catalytic efficiency with 2-methyl-1,2,3,4-tetrahydroquinoline compared to the wild type enzyme
L199T
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the mutation enhances the enzyme activity toward the secondary amines
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the mutant displays an enhanced activity (5-400%) towards most substrates
M226A
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the mutant exhibits enhanced activity relative to the wild type enzyme for most (S)-enantiomers of primary amines and some secondary amines
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the mutant is more active than the wild type enzyme toward the primary amines
M226T
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1.3fold increase of kcat/Km for the substrate L-valine ethyl ester as compared to wild-type enzyme
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the mutant shows reduced catalytic efficiency with (S)-1-phenylethanamine and increased catalytic efficiency with 2-methyl-1,2,3,4-tetrahydroquinoline compared to the wild type enzyme
T198F
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the mutation enhances the enzyme activity toward the secondary amines
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the mutant exhibits 406times higher catalytic efficiency with 2-methyl-1,2,3,4-tetrahydroquinoline than the wild type enzyme. The mutant shows reduced catalytic efficiency with (S)-1-phenylethanamine compared to the wild type enzyme
T198F/L199S/M226F
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the substrate 2-methyl-1, 2, 3, 4-tetrahydroquinoline is deracemized by the triple mutant
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the mutant is more active than the wild type enzyme toward the primary amines
T198I
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2.55fold increase of kcat/Km for the substrate L-valine ethyl ester as compared to wild-type enzyme
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the mutant shows higher catalytic efficiency towards cyclooctanamine compared to the wild type enzyme
Y321A
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the mutation enhances the enzyme activity toward the secondary amines
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the mutant shows higher catalytic efficiency towards cyclooctanamine compared to the wild type enzyme
Y321F
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the mutation enhances the enzyme activity toward the secondary amines
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the mutation enhances the enzyme activity toward the secondary amines and displays an enhanced catalytic efficiency toward 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline
Y321I
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13fold increase of kcat/Km for the substrate L-valine ethyl ester as compared to wild-type enzyme