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Enzyme Nomenclature
Information on EC 1.4.3.12 - cyclohexylamine oxidase
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1.4.3.12 cyclohexylamine oxidaseIUBMB Comments
A flavoprotein (FAD). Some other cyclic amines can act instead of cyclohexylamine, but not simple aliphatic and aromatic amides.
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Word Map
- 1.4.3.12
- oxydans
- brevibacterium
-
deracemization
- flavin
-
deamination
- cyclohexanone
-
monoamine
-
alicyclic
-
chaas
-
prosthetic
-
racemic
- flavoprotein
-
enantiomeric
- monooxygenase
-
biocatalytic
- oxidases
- synthesis
The enzyme appears in viruses and cellular organisms
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
chaA
CHAO
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cyclohexylamine + O2 + H2O = cyclohexanone + NH3 + H2O2
A flavoprotein, FAD. Some other cyclic amines can act instead of cyclohexylamine, but not simple aliphatic and aromatic amides
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
cyclohexylamine:oxygen oxidoreductase (deaminating)
A flavoprotein (FAD). Some other cyclic amines can act instead of cyclohexylamine, but not simple aliphatic and aromatic amides.
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CAS REGISTRY NUMBER
COMMENTARY
63116-97-2
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(1R)-1-(4-chlorophenyl)ethan-1-amine + H2O + O2
1-(4-chlorophenyl)ethanone + NH3 + H2O2
-
-
-
-
?
(1R)-1-phenylethan-1-amine + H2O + O2
1-phenylacetaldehyde + NH3 + H2O2
-
-
-
-
?
(1S)-1-(4-chlorophenyl)ethan-1-amine + H2O + O2
1-(4-chlorophenyl)ethanone + NH3 + H2O2
-
-
-
-
?
(1S)-1-phenylethan-1-amine + H2O + O2
1-phenylacetaldehyde + NH3 + H2O2
-
-
-
-
?
(1S)-1-phenylpropan-1-amine + H2O + O2
1-phenylpropan-1-one + NH3 + H2O2
-
-
-
-
?
(R)-1-(4-chlorophenyl)ethylamine + O2 + H2O
1-(4-chlorophenyl)ethanone + NH3 + H2O2
-
-
-
-
?
(R)-1-(4-fluorophenyl)ethanamine + O2 + H2O
1-(4-fluorophenyl)ethanone + NH3 + H2O2
-
-
-
-
?
(S)-1-(4-chlorophenyl)ethylamine + O2 + H2O
1-(4-chlorophenyl)ethanone + NH3 + H2O2
-
-
-
-
?
(S)-1-(4-fluorophenyl)ethanamine + O2 + H2O
1-(4-fluorophenyl)ethanone + NH3 + H2O2
-
-
-
-
?
(S)-1-p-tolylethanamine + O2 + H2O
1-(4-methylphenyl)ethanone + NH3 + H2O2
-
-
-
-
?
(S)-1-phenylpropan-1-amine + O2 + H2O
1-phenylpropionaldehyde + NH3 + H2O2
-
-
-
-
?
(S)-2-heptylamine + O2 + H2O
heptan-2-one + NH3 + H2O2
-
25% activity compared to cyclohexylamine
-
-
?
(S)-alpha-methylbenzylamine + O2 + H2O
?
-
55% activity compared to cyclohexylamine
-
-
?
1,2,3,4-tetrahydro-2-naphthylamine + O2 + H2O
? + NH3 + H2O2
-
23% of the activity compared to cyclohexylamine
-
?
1,2-cyclohexanediamine + O2 + H2O
cyclohexaneamine + NH3 + H2O2
-
18% of the activity compared to cyclohexylamine
-
?
1-(4-chlorophenyl)ethanamine + O2 + H2O
?
-
35% activity compared to cyclohexylamine
-
-
?
1-(4-fluorophenyl)ethanamine + O2 + H2O
1-(4-fluorophenyl)ethanone + NH3 + H2O2
-
-
-
-
?
1-(4-fluorophenyl)ethanamine + O2 + H2O
?
-
61% activity compared to cyclohexylamine
-
-
?
1-(4-methylphenyl)ethanamine + O2 + H2O
?
-
5% activity compared to cyclohexylamine
-
-
?
1-(4-methylphenyl)methanamine + O2 + H2O
?
-
1% activity compared to cyclohexylamine
-
-
?
1-(naphthalen-1-yl)ethanamine + O2 + H2O
?
-
1% activity compared to cyclohexylamine
-
-
?
1-indanamine + O2 + H2O
1-indanone + NH3 + H2O2
-
27% activity compared to cyclohexylamine
-
-
?
1-phenylethanamine + O2 + H2O
1-phenylacetaldehyde + NH3 + H2O2
-
-
-
-
?
1-phenylethanamine + O2 + H2O
1-phenylethanone + NH3 + H2O2
-
48% activity compared to cyclohexylamine
-
-
?
2-amino-4-phenylbutane + O2 + H2O
4-phenylbutan-2-one + NH3 + H2O2
-
-
-
-
?
2-amino-5-methylhexane + O2 + H2O
5-methylhexane-2-one + NH3 + H2O2
-
-
-
-
?
2-ethyl-1-hexylamine + O2 + H2O
2-ethylhexanaldehyde + NH3 + H2O2
-
-
-
-
?
2-heptylamine + O2 + H2O
heptan-2-one + NH3 + H2O2
-
24% activity compared to cyclohexylamine
-
-
?
2-methyl-1,2,3,4-tetrahydroquinoline + O2 + H2O
(R)-2-methyl-1,2,3,4-tetrahydroquinoline + NH3 + H2O2
2-methylcyclohexanamine + O2 + H2O
2-methylcyclohexanone + NH3 + H2O2
-
-
-
-
?
2-methylcyclohexanamine + O2 + H2O
?
-
56% activity compared to cyclohexylamine
-
-
?
2-methylpropan-1-amine + O2 + H2O
?
-
0.1% activity compared to cyclohexylamine
-
-
?
4-methylbenzylamine + O2 + H2O
4-methylbenzaldehyde + NH3 + H2O2
-
-
-
-
?
4-methylcyclohexylamine + O2 + H2O
?
-
133% activity compared to cyclohexylamine
-
-
?
4-methylpiperidine + O2 + H2O
?
-
0.1% activity compared to cyclohexylamine
-
-
?
4-phenylbutan-2-amine + O2 + H2O
?
-
12% activity compared to cyclohexylamine
-
-
?
5-methylhexan-2-amine + O2 + H2O
?
-
9% activity compared to cyclohexylamine
-
-
?
6-amino-2-methylheptan-2-ol + O2 + H2O
?
-
0.1% activity compared to cyclohexylamine
-
-
?
bicyclo[2.2.1]heptan-2-amine + O2 + H2O
?
-
2% activity compared to cyclohexylamine
-
-
?
butan-2-amine + O2 + H2O
?
-
3% activity compared to cyclohexylamine
-
-
?
cycloheptanamine + O2 + H2O
?
-
75% activity compared to cyclohexylamine
-
-
?
cycloheptylamine + O2 + H2O
cycloheptanone + NH3 + H2O2
-
42% of the activity compared to cyclohexylamine
-
?
cyclooctanamine + O2 + H2O
?
-
23% activity compared to cyclohexylamine
-
-
?
cyclopentylamine + O2 + H2O
cyclohexanone + NH3 + H2O2
-
best substrate
-
-
?
hexan-1-amine + O2 + H2O
?
-
1% activity compared to cyclohexylamine
-
-
?
trans-2-aminocyclohexanol + O2 + H2O
?
-
16% activity compared to cyclohexylamine
-
-
?
(R)-2-heptylamine + O2 + H2O
heptan-2-one + NH3 + H2O2
-
0.1% activity compared to cyclohexylamine
-
-
?
(R)-2-heptylamine + O2 + H2O
heptan-2-one + NH3 + H2O2
-
0.1% activity compared to cyclohexylamine
-
-
?
2-methyl-1,2,3,4-tetrahydroquinoline + O2 + H2O
(R)-2-methyl-1,2,3,4-tetrahydroquinoline + NH3 + H2O2
-
-
-
-
?
2-methyl-1,2,3,4-tetrahydroquinoline + O2 + H2O
(R)-2-methyl-1,2,3,4-tetrahydroquinoline + NH3 + H2O2
-
-
-
-
?
3-phenylpropan-1-amine + H2O + O2
? + NH3 + H2O2
-
7% activity compared to cyclohexylamine
-
-
?
3-phenylpropan-1-amine + H2O + O2
? + NH3 + H2O2
-
7% activity compared to cyclohexylamine
-
-
?
cyclohexylamine + O2 + H2O
cyclohexanone + NH3 + H2O2
-
-
-
-
?
cyclohexylamine + O2 + H2O
cyclohexanone + NH3 + H2O2
-
best substrate
-
-
?
cyclohexylamine + O2 + H2O
cyclohexanone + NH3 + H2O2
-
highly specific for alicyclic monoamines and aliphatic monoamines
-
?
cyclohexylamine + O2 + H2O
cyclohexanone + NH3 + H2O2
-
100% activity
-
-
?
cyclohexylamine + O2 + H2O
cyclohexanone + NH3 + H2O2
-
-
-
-
?
cyclohexylamine + O2 + H2O
cyclohexanone + NH3 + H2O2
-
best substrate
-
-
?
cyclohexylamine + O2 + H2O
cyclohexanone + NH3 + H2O2
-
100% activity
-
-
?
cyclohexylamine + O2 + H2O
cyclohexanone + NH3 + H2O2
-
-
-
-
?
cyclohexylamine + O2 + H2O
cyclohexanone + NH3 + H2O2
-
-
-
?
cyclohexylamine + O2 + H2O
cyclohexanone + NH3 + H2O2
-
highly specific for alicyclic monoamines and aliphatic monoamines
-
?
cyclohexylamine + O2 + H2O
cyclohexanone + NH3 + H2O2
-
-
-
?
cyclohexylamine + O2 + H2O
cyclohexanone + NH3 + H2O2
-
-
-
-
?
cyclohexylamine + O2 + H2O
cyclohexanone + NH3 + H2O2
-
highly specific for alicyclic primary amines, oxygen is the only electron acceptor
-
?
cyclopentylamine + O2 + H2O
cyclopentanone + NH3 + H2O2
-
highly specific for alicyclic monoamines and aliphatic monoamines
-
?
cyclopentylamine + O2 + H2O
cyclopentanone + NH3 + H2O2
-
highly specific for alicyclic monoamines and aliphatic monoamines
-
?
N-methylcyclohexanamine + O2 + H2O
?
-
6% activity compared to cyclohexylamine
-
-
?
N-methylcyclohexylamine + O2 + H2O
cyclohexanone + methylamine + H2O2
-
highly specific for alicyclic monoamines and aliphatic monoamines
-
?
N-methylcyclohexylamine + O2 + H2O
cyclohexanone + methylamine + H2O2
-
highly specific for alicyclic monoamines and aliphatic monoamines
-
?
secondary butylamine + O2 + H2O
butanone + NH3 + H2O2
-
highly specific for alicyclic monoamines and aliphatic monoamines
-
?
secondary butylamine + O2 + H2O
butanone + NH3 + H2O2
-
highly specific for alicyclic monoamines and aliphatic monoamines
-
?
additional information
?
-
-
deracemization of 1-aminotetraline by coupling wild type enzyme with a nonselective reducing agent NH3·BH3 is a route to norsertraline
-
-
?
additional information
?
-
-
no activity with (R)-alpha-methylbenzylamine, 2-methylpiperidine and tetrahydroquinaldine
-
-
?
additional information
?
-
-
trace activity with (R)-2-aminohexane, 1-hexylamine, (R)-(-)-1-phenylethylamine, (R)-1-p-tolylethanamine, (R)-1-aminoindan, (S)-(-)-Nalpha-dimethylbenzylamine, 2-methylpiperidine, 4-methylpiperidine, 2-methyl-1,2,3,4-tetrahydroquinoline, and N,N-dimethylcyclohexylamine. No activity with 1-naphthalen-1-ylethanamine
-
-
?
additional information
?
-
-
when cyclohexylamine oxidase in combination with a borane-ammonia complex as reducing agent is applied to the deracemization of several substrates, excellent enantiomeric ratios (higher than 99:1) and good isolated yields (62-75%) of the corresponding (R)-amines are obtained
-
-
?
additional information
?
-
-
no activitiy towards (R)-N-(prop-2-yn-1-yl)-2, 3-dihydro-1H-inden-1-amine, 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline, (S)-N-methyl-1-phenylethanamine, and 1-methyl-1,2,3,4-tetrahydroisoquinoline
-
-
?
additional information
?
-
-
deracemization of 1-aminotetraline by coupling wild type enzyme with a nonselective reducing agent NH3·BH3 is a route to norsertraline
-
-
?
additional information
?
-
-
trace activity with (R)-2-aminohexane, 1-hexylamine, (R)-(-)-1-phenylethylamine, (R)-1-p-tolylethanamine, (R)-1-aminoindan, (S)-(-)-Nalpha-dimethylbenzylamine, 2-methylpiperidine, 4-methylpiperidine, 2-methyl-1,2,3,4-tetrahydroquinoline, and N,N-dimethylcyclohexylamine. No activity with 1-naphthalen-1-ylethanamine
-
-
?
additional information
?
-
-
no activity with (R)-alpha-methylbenzylamine, 2-methylpiperidine and tetrahydroquinaldine
-
-
?
additional information
?
-
-
when cyclohexylamine oxidase in combination with a borane-ammonia complex as reducing agent is applied to the deracemization of several substrates, excellent enantiomeric ratios (higher than 99:1) and good isolated yields (62-75%) of the corresponding (R)-amines are obtained
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
cyclohexylamine + O2 + H2O
cyclohexanone + NH3 + H2O2
-
-
-
-
?
cyclohexylamine + O2 + H2O
cyclohexanone + NH3 + H2O2
-
best substrate
-
-
?
cyclohexylamine + O2 + H2O
cyclohexanone + NH3 + H2O2
-
highly specific for alicyclic monoamines and aliphatic monoamines
-
?
cyclohexylamine + O2 + H2O
cyclohexanone + NH3 + H2O2
-
100% activity
-
-
?
cyclohexylamine + O2 + H2O
cyclohexanone + NH3 + H2O2
-
best substrate
-
-
?
cyclohexylamine + O2 + H2O
cyclohexanone + NH3 + H2O2
-
100% activity
-
-
?
cyclohexylamine + O2 + H2O
cyclohexanone + NH3 + H2O2
-
-
-
-
?
cyclohexylamine + O2 + H2O
cyclohexanone + NH3 + H2O2
-
-
-
?
cyclohexylamine + O2 + H2O
cyclohexanone + NH3 + H2O2
-
highly specific for alicyclic monoamines and aliphatic monoamines
-
?
cyclohexylamine + O2 + H2O
cyclohexanone + NH3 + H2O2
-
-
-
?
cyclohexylamine + O2 + H2O
cyclohexanone + NH3 + H2O2
-
-
-
-
?
cyclohexylamine + O2 + H2O
cyclohexanone + NH3 + H2O2
-
highly specific for alicyclic primary amines, oxygen is the only electron acceptor
-
?
cyclopentylamine + O2 + H2O
cyclopentanone + NH3 + H2O2
-
highly specific for alicyclic monoamines and aliphatic monoamines
-
?
cyclopentylamine + O2 + H2O
cyclopentanone + NH3 + H2O2
-
highly specific for alicyclic monoamines and aliphatic monoamines
-
?
N-methylcyclohexylamine + O2 + H2O
cyclohexanone + methylamine + H2O2
-
highly specific for alicyclic monoamines and aliphatic monoamines
-
?
N-methylcyclohexylamine + O2 + H2O
cyclohexanone + methylamine + H2O2
-
highly specific for alicyclic monoamines and aliphatic monoamines
-
?
secondary butylamine + O2 + H2O
butanone + NH3 + H2O2
-
highly specific for alicyclic monoamines and aliphatic monoamines
-
?
secondary butylamine + O2 + H2O
butanone + NH3 + H2O2
-
highly specific for alicyclic monoamines and aliphatic monoamines
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
p-chloromercuribenzoate
-
91% inhibition at 0.0005 mM, partially reversed by glutathione
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.66
(S)-1-phenylethanamine
-
mutant enzyme M226F, at pH 6.5 and 30°C
-
0.79
(S)-1-phenylethanamine
-
mutant enzyme Y459T, at pH 6.5 and 30°C
-
0.91
(S)-1-phenylethanamine
-
mutant enzyme L199T, at pH 6.5 and 30°C
-
0.99
(S)-1-phenylethanamine
-
mutant enzyme T198F, at pH 6.5 and 30°C
-
0.99
(S)-1-phenylethanamine
-
mutant enzyme T198F/L199S/M226F, at pH 6.5 and 30°C
-
1.03
(S)-1-phenylethanamine
-
mutant enzyme T198F/L199S, at pH 6.5 and 30°C
-
0.27
2-methyl-1,2,3,4-tetrahydroquinoline
-
mutant enzyme T198F/L199S/M226F, at pH 6.5 and 30°C
-
0.29
2-methyl-1,2,3,4-tetrahydroquinoline
-
mutant enzyme Y459T, at pH 6.5 and 30°C
-
0.36
2-methyl-1,2,3,4-tetrahydroquinoline
-
mutant enzyme T198F/L199S, at pH 6.5 and 30°C
-
0.62
2-methyl-1,2,3,4-tetrahydroquinoline
-
mutant enzyme M226F, at pH 6.5 and 30°C
-
0.69
2-methyl-1,2,3,4-tetrahydroquinoline
-
mutant enzyme T198F, at pH 6.5 and 30°C
-
1.06
2-methyl-1,2,3,4-tetrahydroquinoline
-
wild type enzyme, at pH 6.5 and 30°C
-
1.12
2-methyl-1,2,3,4-tetrahydroquinoline
-
mutant enzyme L199T, at pH 6.5 and 30°C
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.16
(S)-1-phenylethanamine
-
mutant enzyme Y459T, at pH 6.5 and 30°C
-
0.19
(S)-1-phenylethanamine
-
mutant enzyme T198F/L199S/M226F, at pH 6.5 and 30°C
-
0.29
(S)-1-phenylethanamine
-
mutant enzyme T198F/L199S, at pH 6.5 and 30°C
-
0.76
(S)-1-phenylethanamine
-
mutant enzyme L199T, at pH 6.5 and 30°C
-
1.4
(S)-1-phenylethanamine
-
mutant enzyme T198F, at pH 6.5 and 30°C
-
1.55
(S)-1-phenylethanamine
-
mutant enzyme M226F, at pH 6.5 and 30°C
-
0.003
2-methyl-1,2,3,4-tetrahydroquinoline
-
wild type enzyme, at pH 6.5 and 30°C
-
0.06
2-methyl-1,2,3,4-tetrahydroquinoline
-
mutant enzyme M226F, at pH 6.5 and 30°C
-
0.15
2-methyl-1,2,3,4-tetrahydroquinoline
-
mutant enzyme T198F, at pH 6.5 and 30°C
-
0.23
2-methyl-1,2,3,4-tetrahydroquinoline
-
mutant enzyme L199T, at pH 6.5 and 30°C
-
0.25
2-methyl-1,2,3,4-tetrahydroquinoline
-
mutant enzyme T198F/L199S, at pH 6.5 and 30°C
-
0.27
2-methyl-1,2,3,4-tetrahydroquinoline
-
mutant enzyme Y459T, at pH 6.5 and 30°C
-
0.31
2-methyl-1,2,3,4-tetrahydroquinoline
-
mutant enzyme T198F/L199S/M226F, at pH 6.5 and 30°C
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.19
(S)-1-phenylethanamine
-
mutant enzyme T198F/L199S/M226F, at pH 6.5 and 30°C
-
0.21
(S)-1-phenylethanamine
-
mutant enzyme Y459T, at pH 6.5 and 30°C
-
0.28
(S)-1-phenylethanamine
-
mutant enzyme T198F/L199S, at pH 6.5 and 30°C
-
0.84
(S)-1-phenylethanamine
-
mutant enzyme L199T, at pH 6.5 and 30°C
-
1.42
(S)-1-phenylethanamine
-
mutant enzyme T198F, at pH 6.5 and 30°C
-
2.35
(S)-1-phenylethanamine
-
mutant enzyme M226F, at pH 6.5 and 30°C
-
0.003
2-methyl-1,2,3,4-tetrahydroquinoline
-
wild type enzyme, at pH 6.5 and 30°C
-
0.1
2-methyl-1,2,3,4-tetrahydroquinoline
-
mutant enzyme M226F, at pH 6.5 and 30°C
-
0.2
2-methyl-1,2,3,4-tetrahydroquinoline
-
mutant enzyme L199T, at pH 6.5 and 30°C
-
0.22
2-methyl-1,2,3,4-tetrahydroquinoline
-
mutant enzyme T198F, at pH 6.5 and 30°C
-
0.68
2-methyl-1,2,3,4-tetrahydroquinoline
-
mutant enzyme T198F/L199S, at pH 6.5 and 30°C
-
0.92
2-methyl-1,2,3,4-tetrahydroquinoline
-
mutant enzyme Y459T, at pH 6.5 and 30°C
-
1.15
2-methyl-1,2,3,4-tetrahydroquinoline
-
mutant enzyme T198F/L199S/M226F, at pH 6.5 and 30°C
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.013
-
with 2-ethyl-1-hexylamine as substrate, wild type enzyme, at pH 6.5 and 30°C
0.018
-
with (R)-1-(4-chlorophenyl)ethylamine as substrate, wild type enzyme, at pH 6.5 and 30°C
0.08
-
with N-methylcyclohexanamine as substrate, wild type enzyme, at pH 6.5 and 30°C
0.084
-
with (R)-1-(4-fluorophenyl)ethanamine as substrate, wild type enzyme, at pH 6.5 and 30°C
0.11
-
with 4-methylbenzylamine as substrate, wild type enzyme, at pH 6.5 and 30°C
0.27
-
with (S)-1-p-tolylethanamine as substrate, wild type enzyme, at pH 6.5 and 30°C
0.33
-
with cyclopentylamine as substrate, wild type enzyme, at pH 6.5 and 30°C
0.34
-
with benzylamine as substrate, wild type enzyme, at pH 6.5 and 30°C
0.68
-
with 2-amino-4-phenylbutane as substrate, wild type enzyme, at pH 6.5 and 30°C
0.97
-
with 2-aminocyclohexanol as substrate, wild type enzyme, at pH 6.5 and 30°C
1.033
-
with cyclooctanamine as substrate, wild type enzyme, at pH 6.5 and 30°C
1.13
-
with 2-aminopentane as substrate, wild type enzyme, at pH 6.5 and 30°C
1.2
-
with 2-aminoheptane as substrate, wild type enzyme, at pH 6.5 and 30°C
1.49
-
with 2-aminonorbornane hydrochloride as substrate, wild type enzyme, at pH 6.5 and 30°C
1.66
-
with (S)-1-phenylpropropan-1-amine as substrate, wild type enzyme, at pH 6.5 and 30°C
2.35
-
with (S)-1-aminoindan as substrate, wild type enzyme, at pH 6.5 and 30°C
2.36
-
with 1-phenylethanamine as substrate, wild type enzyme, at pH 6.5 and 30°C
2.62
-
with (S)-1-(4-chlorophenyl)ethylamine as substrate, wild type enzyme, at pH 6.5 and 30°C
2.79
-
with (S)-2-aminohexane as substrate, wild type enzyme, at pH 6.5 and 30°C
3.058
-
with 2-methylcyclohexanamine as substrate, wild type enzyme, at pH 6.5 and 30°C
3.37
-
with 1-(4-fluorophenyl)ethanamine as substrate, wild type enzyme, at pH 6.5 and 30°C
3.51
-
with (S)-(-)-1-phenylethylamine as substrate, wild type enzyme, at pH 6.5 and 30°C
3.6
-
with 2-amino-5-methylhexane as substrate, wild type enzyme, at pH 6.5 and 30°C
4.56
-
with (S)-1-(4-fluorophenyl)ethanamine as substrate, wild type enzyme, at pH 6.5 and 30°C
5.6
-
with cyclohexylamine as substrate, wild type enzyme, at pH 6.5 and 30°C
5.69
-
with (S)-1-aminotetraline as substrate, wild type enzyme, at pH 6.5 and 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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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). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
flavoprotein
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 30% (w/v) PEG 8000 and 0.2 M sodium acetate trihydrate in 0.1 M sodium cacodylate pH 6.5
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
L199A
-
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
-
the mutant is more active than the wild type enzyme toward the primary amines
L199I
-
the mutant is more active than the wild type enzyme toward the primary amines
L199T
L353M
-
the mutant shows 7-445% higher activity towards primary aliphatic amines with cycloalkane or aromatic moieties
M226A
M226F
-
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
-
the mutant is more active than the wild type enzyme toward the primary amines
M226T
-
the mutant is more active than the wild type enzyme toward the primary amines
T198A
-
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
-
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
-
the mutant is more active than the wild type enzyme toward the primary amines
Y321A
Y321F
Y321I
-
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/M226T
-
the double mutant acts on (S)-N-(prop-2-yn-1-yl)-2,3-dihydro-1H-inden-1-amine
Y321T
-
the mutation enhances the enzyme activity toward the secondary amines
Y459T
-
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
-
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
L199T
-
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
L353M
-
the mutant shows 7-445% higher activity towards primary aliphatic amines with cycloalkane or aromatic moieties
M226A
-
the mutant displays an enhanced activity (5-400%) towards most substrates
M226F
-
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
-
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/L199S
-
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
-
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
Y321A
-
the mutant shows higher catalytic efficiency towards cyclooctanamine compared to the wild type enzyme
Y321F
-
the mutant shows higher catalytic efficiency towards cyclooctanamine compared to the wild type enzyme
L199T
-
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
-
the mutation enhances the enzyme activity toward the secondary amines
M226A
-
the mutant displays an enhanced activity (5-400%) towards most substrates
M226A
-
the mutant exhibits enhanced activity relative to the wild type enzyme for most (S)-enantiomers of primary amines and some secondary amines
T198F
-
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
-
the mutation enhances the enzyme activity toward the secondary amines
T198F/L199S/M226F
-
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
-
the substrate 2-methyl-1, 2, 3, 4-tetrahydroquinoline is deracemized by the triple mutant
Y321A
-
the mutant shows higher catalytic efficiency towards cyclooctanamine compared to the wild type enzyme
Y321A
-
the mutation enhances the enzyme activity toward the secondary amines
Y321F
-
the mutant shows higher catalytic efficiency towards cyclooctanamine compared to the wild type enzyme
Y321F
-
the mutation enhances the enzyme activity toward the secondary amines
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9
-
the enzyme retains more than 70% of its original activity over a broad range of pH 6.0–9.0 at 4°C for 24 h. However, stability decreases quickly in more acidic condition
724095
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
-
the wild type enzyme is stable at 40°C for at least 30 min, but decreases rapidly above 40°C
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE cellulose DE-52 column chromatography, and Toyopearl Butyl-650S column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 cells
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
-
the enzyme is a useful biocatalyst for the kinetic resolution and dereacemization of amines
synthesis
-
the enzyme is a useful biocatalyst for the kinetic resolution and dereacemization of amines
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tokieda, T.; Niimura, T.; Takamura,F.; Yamaha, T.
Purification and some properties of cyclohexylamine oxidase from a Pseudomonas sp.
J. Biochem.
81
851-858
1977
Pseudomonas sp.
brenda
Iwaki, H.; Shimizu, M.; Tokuyama, T.; Hasegawa, Y.
Biodegradation of cyclohexylamine by Brevibacterium oxydans IH-35A
Appl. Environ. Microbiol.
65
2232-2234
1999
Microbacterium oxydans, Microbacterium oxydans IH-35A
brenda
Iwaki, H.; Shimizu, M.; Tokuyama, T.; Hasegawa, Y.
Purification and characterization of a novel cyclohexylamine oxidase from the cyclohexylamine-degrading Brevibacterium oxydans IH-35A
J. Biosci. Bioeng.
88
264-268
1999
Microbacterium oxydans, Microbacterium oxydans IH-35A
brenda
Li, G.; Ren, J.; Iwaki, H.; Zhang, D.; Hasegawa, Y.; Wu, Q.; Feng, J.; Lau, P.C.; Zhu, D.
Substrate profiling of cyclohexylamine oxidase and its mutants reveals new biocatalytic potential in deracemization of racemic amines
Appl. Microbiol. Biotechnol.
98
1681-1689
2014
Microbacterium oxydans, Microbacterium oxydans IH-35A
brenda
Leisch, H.; Grosse, S.; Iwaki, H.; Hasegawa, Y.; Lau, P.
Cyclohexylamine oxidase as a useful biocatalyst for the kinetic resolution and dereacemization of amines
Can. J. Chem.
90
39-45
2012
Microbacterium oxydans, Microbacterium oxydans IH-35A
-
brenda
Mirza, I.A.; Burk, D.L.; Xiong, B.; Iwaki, H.; Hasegawa, Y.; Grosse, S.; Lau, P.C.; Berghuis, A.M.
Structural analysis of a novel cyclohexylamine oxidase from Brevibacterium oxydans IH-35A
PLoS ONE
8
e60072
2013
Microbacterium oxydans (M5AWH1), Microbacterium oxydans, Microbacterium oxydans IH-35A (M5AWH1)
brenda
Li, G.; Ren, J.; Yao, P.; Duan, Y.; Zhang, H.; Wu, Q.; Feng, J.; Lau, P.; Zhu, D.
Deracemization of 2-methyl-1,2,3,4-tetrahydroquinoline using mutant cyclohexylamine oxidase obtained by iterative saturation mutagenesis
ACS Catal.
4
903-908
2014
Microbacterium oxydans, Microbacterium oxydans IH-35A
-
brenda
Yan, D.Z.; Li, X.; Li, C.Z.; Mao, L.Q.; Chi, X.Q.; Zhou, N.Y.; Liu, D.Y.
Genome-wide identification and characterization of genes encoding cyclohexylamine degradation in a novel cyclohexylamine-degrading bacterial strain of Pseudomonas plecoglossicida NyZ12
J. Biotechnol.
251
166-173
2017
Pseudomonas plecoglossicida, Pseudomonas plecoglossicida NyZ12
brenda
Li, G.; Yao, P.; Cong, P.; Ren, J.; Wang, L.; Feng, J.; Lau, P.C.; Wu, Q.; Zhu, D.
New recombinant cyclohexylamine oxidase variants for deracemization of secondary amines by orthogonally assaying designed mutants with structurally diverse substrates
Sci. Rep.
6
24973
2016
Microbacterium oxydans
brenda
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