HOME
login
history
all enzymes
BRENDA home
History
Information on EC 1.4.3.12 - cyclohexylamine oxidase
for references in articles please use BRENDA:EC1.4.3.12Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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.
Specify your search results
Word Map
- 1.4.3.12
-
chaos
- oxydans
- brevibacterium
-
alicyclic
- cyclohexanone
-
monoamine
- flavin
-
deracemization
-
deamination
-
prosthetic
-
biocatalytic
- oxidases
- flavoprotein
- monooxygenase
- synthesis
The enzyme appears in viruses and cellular organisms
Synonyms
chaA, CHAO, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
chaA
CHAO
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cyclohexylamine + O2 + H2O = cyclohexanone + NH3 + H2O2
a flavoprotein, FAD; A flavoprotein, FAD. Some other cyclic amines can act instead of cyclohexylamine, but not simple aliphatic and aromatic amides
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
oxidative deamination
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
63116-97-2
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
M5AWH1
-
-
-
?
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
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
p-chloromercuribenzoate
-
91% inhibition at 0.0005 mM, partially reversed by glutathione
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.08
(S)-1-aminotetraline
-
mutant enzyme Y321A, at pH 6.5 and 30°C; wild type enzyme, at pH 6.5 and 30°C
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; 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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
inducible by growth on cyclohexylamine; inducible by growth on cyclohexylamine
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
flavoprotein
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
DEAE cellulose DE-52 column chromatography, and Toyopearl Butyl-650S column chromatography
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 1.4.3.12)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Information
