We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments The enzyme from Bacillus sp. OxB-1 contains protoheme IX, the iron of which must be in the form iron(II) for activity. (Z)-Phenylacetaldoxime binds to ferric heme (the iron(III) form) via the oxygen atom whereas it binds to the active ferrous form via the nitrogen atom. In this way, the oxidation state of the heme controls the coordination stucture of the substrate---heme complex, which regulates enzyme activity . The enzyme is active towards several (Z)-arylacetaldoximes and (E/Z)-alkylaldoximes as well as towards arylalkylaldoximes such as 3-phenylpropionaldoxime and 4-phenylbutyraldoxime. However, it is inactive with phenylacetaldoximes that have a substituent group at an alpha-site of an oxime group, for example, with (E/Z)-2-phenylpropionaldoxime and (E/Z)-mandelaldoxime. The activity of the enzyme is inhibited completely by the heavy-metal cations Cu+, Cu2+, Ag+ and Hg+ whereas Fe2+ and Sn2+ have an activatory effect.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
aldoxime dehydratase, OXD, OxdB, OxdFG, OxdRE, phenylacetaldoxime dehydratase,
UP10_21065 ,
more
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
phenylacetaldoxime dehydratase
aldoxime dehydratase
-
OXD
-
OxdB
-
-
OxdFG
-
phenylacetaldoxime dehydratase
-
phenylacetaldoxime dehydratase
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(Z)-phenylacetaldehyde oxime = phenylacetonitrile + H2O
(Z)-phenylacetaldehyde oxime = phenylacetonitrile + H2O
-
-
-
-
(Z)-phenylacetaldehyde oxime = phenylacetonitrile + H2O
oxidation state of heme controls the coordination structure of a substrate-hem complex, which regulates enzyme activity
-
(Z)-phenylacetaldehyde oxime = phenylacetonitrile + H2O
oxidation state of heme controls the coordination structure of a substrate-hem complex, which regulates enzyme activity
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(Z)-phenylacetaldehyde-oxime hydro-lyase (phenylacetonitrile-forming)
The enzyme from Bacillus sp. OxB-1 contains protoheme IX, the iron of which must be in the form iron(II) for activity. (Z)-Phenylacetaldoxime binds to ferric heme (the iron(III) form) via the oxygen atom whereas it binds to the active ferrous form via the nitrogen atom. In this way, the oxidation state of the heme controls the coordination stucture of the substrate---heme complex, which regulates enzyme activity [2]. The enzyme is active towards several (Z)-arylacetaldoximes and (E/Z)-alkylaldoximes as well as towards arylalkylaldoximes such as 3-phenylpropionaldoxime and 4-phenylbutyraldoxime. However, it is inactive with phenylacetaldoximes that have a substituent group at an alpha-site of an oxime group, for example, with (E/Z)-2-phenylpropionaldoxime and (E/Z)-mandelaldoxime. The activity of the enzyme is inhibited completely by the heavy-metal cations Cu+, Cu2+, Ag+ and Hg+ whereas Fe2+ and Sn2+ have an activatory effect.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(E/Z)-2-phenylpropionaldoxime
(E/Z)-2-phenylpropiononitrile + H2O
-
-
-
?
(E/Z)-2-phenylpropionaldoxime
2-phenylpropiononitrile + H2O
17% of the activity with (E/Z)-phenylacetaldehyde oxime
-
-
?
(E/Z)-3-phenylpropionaldoxime
3-phenylpropiononitrile + H2O
131% of the activity with (E/Z)-phenylacetaldehyde oxime
-
-
?
(E/Z)-4-phenylbutyraldoxime
(E/Z)-4-phenylbutyronitrile + H2O
-
-
-
?
(E/Z)-4-phenylbutyraldoxime
phenylbutyronitrile + H2O
(E/Z)-indole-3-acetaldoxime
indole-3-acetonitrile + H2O
10% of the activity with (E/Z)-phenylacetaldehyde oxime
-
-
?
(E/Z)-indoleacetaldoxime
(E/Z)-indoleacetonitrile + H2O
-
-
-
?
(E/Z)-indoleacetaldoxime
indoleacetonitrile + H2O
(E/Z)-isocapronaldoxime
isocapronitrile + H2O
-
29.4% of activity with (Z)-phenylacetaldehyde oxime
-
-
?
(E/Z)-isovaleraldoxime
isovaleronitrile + H2O
(E/Z)-mandelaldoxime
(E/Z)-mandeloacetonitrile + H2O
-
-
-
?
(E/Z)-n-butyraldoxime
n-butyronitrile + H2O
(E/Z)-n-capronaldoxime
n-capronitrile + H2O
-
57.1% of activity with (Z)-phenylacetaldehyde oxime
-
-
?
(E/Z)-n-capronaldoxime
n-caprononitrile + H2O
(E/Z)-n-valeraldoxime
n-valeronitrile + H2O
(E/Z)-phenylacetaldehyde oxime
phenylacetonitrile + H2O
-
-
-
?
(E/Z)-propionaldoxime
propionitrile + H2O
(Z)-3-phenylpropionaldoxime
3-phenylpropionitrile + H2O
(Z)-3-phenylpropionaldoxime
phenylpropionitrile + H2O
-
63% of activity with (Z)-phenylacetaldehyde oxime
-
-
?
(Z)-naphthoacetaldoxime
naphthoacetonitrile + H2O
-
4.5% of activity with (Z)-phenylacetaldehyde oxime
-
-
?
(Z)-p-chlorophenylacetaldoxime
p-chlorophenylacetonitrile + H2O
-
7.3% of activity with (Z)-phenylacetaldehyde oxime
-
-
?
(Z)-p-methoxyphenylacetaldoxime
p-methoxyphenylacetonitrile + H2O
-
6.8% of activity with (Z)-phenylacetaldehyde oxime
-
-
?
(Z)-phenylacetaldehyde oxime
phenylacetonitrile + H2O
(Z)-phenylacetaldoxime
phenylacetonitrile + H2O
Z-3-phenylpropionaldoxime
Z-3-phenylpropiononitrile + H2O
-
-
-
?
(E/Z)-4-phenylbutyraldoxime
phenylbutyronitrile + H2O
-
6.8% of activity with (Z)-phenylacetaldehyde oxime
-
-
?
(E/Z)-4-phenylbutyraldoxime
phenylbutyronitrile + H2O
-
6.8% of activity with (Z)-phenylacetaldehyde oxime
-
-
?
(E/Z)-indoleacetaldoxime
indoleacetonitrile + H2O
-
18.1% of activity with (Z)-phenylacetaldehyde oxime
-
-
?
(E/Z)-indoleacetaldoxime
indoleacetonitrile + H2O
-
18.1% of activity with (Z)-phenylacetaldehyde oxime
-
-
?
(E/Z)-isovaleraldoxime
isovaleronitrile + H2O
-
20.2% of activity with (Z)-phenylacetaldehyde oxime
-
-
?
(E/Z)-isovaleraldoxime
isovaleronitrile + H2O
-
20.2% of activity with (Z)-phenylacetaldehyde oxime
-
-
?
(E/Z)-isovaleraldoxime
isovaleronitrile + H2O
14% of the activity with (E/Z)-phenylacetaldehyde oxime
-
-
?
(E/Z)-isovaleraldoxime
isovaleronitrile + H2O
-
-
-
?
(E/Z)-isovaleraldoxime
isovaleronitrile + H2O
-
-
-
?
(E/Z)-n-butyraldoxime
n-butyronitrile + H2O
-
11% of activity with (Z)-phenylacetaldehyde oxime
-
-
?
(E/Z)-n-butyraldoxime
n-butyronitrile + H2O
-
11% of activity with (Z)-phenylacetaldehyde oxime
-
-
?
(E/Z)-n-butyraldoxime
n-butyronitrile + H2O
12% of the activity with (E/Z)-phenylacetaldehyde oxime
-
-
?
(E/Z)-n-butyraldoxime
n-butyronitrile + H2O
-
-
-
?
(E/Z)-n-butyraldoxime
n-butyronitrile + H2O
-
-
-
?
(E/Z)-n-capronaldoxime
n-caprononitrile + H2O
-
-
-
?
(E/Z)-n-capronaldoxime
n-caprononitrile + H2O
-
-
-
?
(E/Z)-n-valeraldoxime
n-valeronitrile + H2O
-
39.3% of activity with (Z)-phenylacetaldehyde oxime
-
-
?
(E/Z)-n-valeraldoxime
n-valeronitrile + H2O
-
39.3% of activity with (Z)-phenylacetaldehyde oxime
-
-
?
(E/Z)-n-valeraldoxime
n-valeronitrile + H2O
55% of the activity with (E/Z)-phenylacetaldehyde oxime
-
-
?
(E/Z)-n-valeraldoxime
n-valeronitrile + H2O
-
-
-
?
(E/Z)-n-valeraldoxime
n-valeronitrile + H2O
-
-
-
?
(E/Z)-propionaldoxime
propionitrile + H2O
-
8.2% of activity with (Z)-phenylacetaldehyde oxime
-
-
?
(E/Z)-propionaldoxime
propionitrile + H2O
5% of the activity with (E/Z)-phenylacetaldehyde oxime
-
-
?
(Z)-3-phenylpropionaldoxime
3-phenylpropionitrile + H2O
-
-
quantitative yield of product
-
?
(Z)-3-phenylpropionaldoxime
3-phenylpropionitrile + H2O
-
-
quantitative yield of product
-
?
(Z)-phenylacetaldehyde oxime
phenylacetonitrile + H2O
-
-
-
-
?
(Z)-phenylacetaldehyde oxime
phenylacetonitrile + H2O
-
-
-
?
(Z)-phenylacetaldehyde oxime
phenylacetonitrile + H2O
-
-
-
?
(Z)-phenylacetaldehyde oxime
phenylacetonitrile + H2O
-
-
-
-
?
(Z)-phenylacetaldehyde oxime
phenylacetonitrile + H2O
-
-
-
?
(Z)-phenylacetaldehyde oxime
phenylacetonitrile + H2O
-
-
-
?
(Z)-phenylacetaldehyde oxime
phenylacetonitrile + H2O
-
-
-
?
(Z)-phenylacetaldoxime
phenylacetonitrile + H2O
-
-
-
?
(Z)-phenylacetaldoxime
phenylacetonitrile + H2O
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(Z)-phenylacetaldehyde oxime
phenylacetonitrile + H2O
(Z)-phenylacetaldehyde oxime
phenylacetonitrile + H2O
-
-
-
?
(Z)-phenylacetaldehyde oxime
phenylacetonitrile + H2O
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
FMN
-
required
FMN
-
absolute requirement
heme
-
protoheme IX
heme
-
active state contains ferrous heme
heme
-
both the Fe(II) and Fe(III) hemes in OxdB bind the substrate, (Z)-phenylacetaldehyde oxime, using a different coordination mode. Ferrous OxdB is active, but ferric OxdB is not
heme
-
ferrous enzyme includes a five-coordinate high-spin heme to which the substrate is bound via its nitrogen atom for the reaction to occur. Although the ferric enzyme is inactive for catalysis, the substrate is bound to the ferric heme via its oxygen atom
heme
-
ferrous enzyme includes a five-coordinate high-spin heme to which the substrate is bound via its nitrogen atom for the reaction to occur. Although the ferric enzyme is inactive for catalysis, the substrate is bound to the ferric heme via its oxygen atom
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
sulfite
-
substitutes for FMN, to a low degree
additional information
-
up to 5fold enhancement of activity with FMN under anaerobic conditions
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Dehydration
Regulation of aldoxime dehydratase activity by redox-dependent change in the coordination structure of the aldoxime-heme complex.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3.71
(E/Z)-2-phenylpropionaldoxime
-
5.24
(E/Z)-4-phenylbutyraldoxime
-
pH 7.0, 30°C
1.46 - 2.4
(E/Z)-indoleacetaldoxime
2.98
(E/Z)-isocapronaldoxime
-
pH 7.0, 30°C
2.66 - 3.58
(E/Z)-isovaleraldoxime
1.7
(E/Z)-mandelaldoxime
-
2.87 - 11.1
(E/Z)-n-butyraldoxime
0.802 - 6.12
(E/Z)-n-capronaldoxime
2.42 - 10.1
(E/Z)-n-valeraldoxime
4.32
(E/Z)-propionaldoxime
-
pH 7.0, 30°C
1.36 - 2.76
(Z)-3-phenylpropionaldoxime
0.846
(Z)-naphthoacetaldoxime
-
pH 7.0, 30°C
1.24
(Z)-p-chlorophenylacetaldoxime
-
pH 7.0, 30°C
3.08
(Z)-p-methoxyphenylacetaldoxime
-
pH 7.0, 30°C
0.03 - 3.52
(Z)-phenylacetaldehyde oxime
0.38 - 2.52
(Z)-phenylacetaldoxime
1.79
4-phenylbutanal oxime
-
1.46
(E/Z)-indoleacetaldoxime
-
2.4
(E/Z)-indoleacetaldoxime
-
pH 7.0, 30°C
3.58
(E/Z)-isovaleraldoxime
-
pH 7.0, 30°C
2.66
(E/Z)-isovaleraldoxime
-
2.87
(E/Z)-n-butyraldoxime
-
11.1
(E/Z)-n-butyraldoxime
-
pH 7.0, 30°C
0.802
(E/Z)-n-capronaldoxime
-
6.12
(E/Z)-n-capronaldoxime
-
pH 7.0, 30°C
10.1
(E/Z)-n-valeraldoxime
-
-
2.42
(E/Z)-n-valeraldoxime
-
pH 7.0, 30°C
10.1
(E/Z)-n-valeraldoxime
-
2.76
(Z)-3-phenylpropionaldoxime
-
1.36
(Z)-3-phenylpropionaldoxime
-
pH 7.0, 30°C
3.52
(Z)-phenylacetaldehyde oxime
-
0.031
(Z)-phenylacetaldehyde oxime
-
pH.0, 30°C, anaerobic conditions
0.03
(Z)-phenylacetaldehyde oxime
-
pH.0, 30°C, aerobic conditions
0.31
(Z)-phenylacetaldehyde oxime
-
pH.0, 30°C, aerobic conditions, Na2SO3 substitutes for FMN
0.872
(Z)-phenylacetaldehyde oxime
-
pH 7.0, 30°C
0.7
(Z)-phenylacetaldoxime
-
wild type
0.38
(Z)-phenylacetaldoxime
H282G mutant in the presence of pyridine
0.46
(Z)-phenylacetaldoxime
H282G mutant in the presence of 4-chloropyridine
0.47
(Z)-phenylacetaldoxime
H282G mutant in the presence of 4-methylimidazole
0.48
(Z)-phenylacetaldoxime
H282G mutant in the presence of 4-acetylpyridine
0.67
(Z)-phenylacetaldoxime
H282G mutant in the presence of 4-methylpyridine
0.7
(Z)-phenylacetaldoxime
wild type
1.64
(Z)-phenylacetaldoxime
-
H282G mutant in the presence of 4-methoxypyridine
0.76
(Z)-phenylacetaldoxime
H282G mutant in the presence of imidazole
0.78
(Z)-phenylacetaldoxime
H282G mutant in the presence of 1-methylimidazole
2.52
(Z)-phenylacetaldoxime
H282G mutant in the presence of 1-vinylimidazole
1.1
(Z)-phenylacetaldoxime
H282G mutant in the presence of 2-methylimidazole
1.64
(Z)-phenylacetaldoxime
H282G mutant in the presence of 4-methoxypyridine
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5.5
activity with (Z)-phenylacetaldehyde oxime
7
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
UniProt
brenda
MAFF305135
SwissProt
brenda
MAFF305135
SwissProt
brenda
N-771
-
-
brenda
-
-
-
brenda
-
SwissProt
brenda
enzyme expressed in Escherichia coli
-
-
brenda
enzyme expression in Escherichia coli and Bacillus subtilis
-
-
brenda
induction by substrate
-
-
brenda
-
-
-
brenda
-
SwissProt
brenda
enzyme expressed in Escherichia coli
-
-
brenda
enzyme expression in Escherichia coli and Bacillus subtilis
-
-
brenda
induction by substrate
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
-
brenda
-
-
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
OXD_BACSX
Bacillus sp. (strain OxB-1)
351
0
40151
Swiss-Prot
-
H0TG19_9BRAD
342
0
38296
TrEMBL
-
A0A378TIJ4_9MYCO
357
0
40314
TrEMBL
-
A0A6N0Z2Y4_9GAMM
352
0
40991
TrEMBL
-
A0A1X1PFP6_9BURK
352
0
39970
TrEMBL
-
B1Z4N0_BURA4
Burkholderia ambifaria (strain MC40-6)
350
0
39798
TrEMBL
-
A0A120G0G2_PSEFL
352
0
39972
TrEMBL
-
A0A128F083_9GAMM
339
0
38474
TrEMBL
-
A0A2J7VZ61_9BURK
352
0
39300
TrEMBL
-
A0A4U9D051_RAOTE
374
0
43500
TrEMBL
-
E6WMT6_PANSA
Pantoea sp. (strain At-9b)
348
0
39765
TrEMBL
-
C5CLD2_VARPS
Variovorax paradoxus (strain S110)
305
0
34022
TrEMBL
-
A0A1F2PSC5_RHOER
353
0
39511
TrEMBL
-
A5W3Z8_PSEP1
Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1)
352
0
39977
TrEMBL
-
A0A5E6VP91_PSEFL
352
0
39970
TrEMBL
-
J7LVR2_9MICC
366
0
40542
TrEMBL
-
C5CKL2_VARPS
Variovorax paradoxus (strain S110)
353
0
39100
TrEMBL
-
A0A2U3MXR0_9GAMM
346
0
40249
TrEMBL
-
A0A0J6F2S8_9BORD
352
0
40274
TrEMBL
-
A0A508TMR7_9BRAD
349
0
38728
TrEMBL
-
A0A5M9I9Z1_PSEPA
352
0
39991
TrEMBL
-
K9NMZ4_9PSED
352
0
40286
TrEMBL
-
A0A6P2ERG9_9BURK
352
0
39325
TrEMBL
-
E6UV59_VARPE
Variovorax paradoxus (strain EPS)
353
0
39810
TrEMBL
-
A5V4Y9_SPHWW
Sphingomonas wittichii (strain RW1 / DSM 6014 / JCM 10273)
343
0
38752
TrEMBL
-
A0A454G6H4_PSESF
293
0
32752
TrEMBL
-
A0A2Z2NIZ7_9GAMM
340
0
37831
TrEMBL
-
B1K8P0_BURCC
Burkholderia cenocepacia (strain MC0-3)
352
0
39985
TrEMBL
-
A0A5E4SMD2_9BURK
352
0
40247
TrEMBL
-
A0A0H4W9V0_9BORD
352
0
40273
TrEMBL
-
A0A5E6QQ07_PSEFL
352
0
40064
TrEMBL
-
A0A5E7EJM3_PSEFL
352
0
40053
TrEMBL
-
A0A7H4N485_KLEVA
349
0
39362
TrEMBL
-
W6VN61_PSESZ
Pseudomonas sp. (strain GM41(2012))
352
0
40193
TrEMBL
-
B1KM99_SHEWM
Shewanella woodyi (strain ATCC 51908 / MS32)
332
0
38259
TrEMBL
-
A0A128F5A6_9GAMM
339
0
38611
TrEMBL
-
A0A5M9J2J8_9PSED
352
0
40156
TrEMBL
-
A5EKU7_BRASB
Bradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182)
340
0
38026
TrEMBL
-
A0A679J942_VARPD
351
0
39743
TrEMBL
-
A0A5E7UGE5_PSEFL
346
0
39619
TrEMBL
-
A0A5E7A567_PSEFL
352
0
40151
TrEMBL
-
A0A5E7GES2_PSEFL
352
0
40359
TrEMBL
-
F0QD95_ACIAP
Acidovorax avenae (strain ATCC 19860 / DSM 7227 / JCM 20985 / NCPPB 1011)
353
0
40033
TrEMBL
-
A0A0D8I6C2_RHOSX
Rhodococcus sp. (strain AD45)
357
0
40578
TrEMBL
-
A0A1Q9QYR2_PSEPU
346
0
39244
TrEMBL
-
A0A5P9F157_9GAMM
324
0
36713
TrEMBL
-
A7IFL4_XANP2
Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2)
347
0
39408
TrEMBL
-
A0A5E6RJ84_PSEFL
352
0
39947
TrEMBL
-
A0A0H2LS71_VARPD
353
0
39192
TrEMBL
-
A0A0T9RLB6_9GAMM
346
0
39807
TrEMBL
-
A0A5E7UNM2_PSEFL
352
0
40327
TrEMBL
-
A0A679JQU0_9RHIZ
350
0
40020
TrEMBL
-
E2XQ72_PSEFL
186
0
20681
TrEMBL
-
E2XQ71_PSEFL
166
0
18787
TrEMBL
-
A0A7Z8ZAG1_RAOTE
342
0
39432
TrEMBL
-
B1FI60_9BURK
350
0
39797
TrEMBL
-
A0A509E8I8_9RHIZ
317
0
36069
TrEMBL
-
A0A379L151_PSEPU
352
0
39756
TrEMBL
-
A0A5E7DBG3_PSEFL
352
0
40283
TrEMBL
-
C6WDR0_ACTMD
Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU 3971)
343
0
37727
TrEMBL
-
A0A0D7Q864_9BRAD
345
0
38550
TrEMBL
-
Q2WG72_GIBZA
363
0
41217
TrEMBL
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
monomer
-
1 * 40000, SDS-PAGE
monomer
-
1 * 40000, SDS-PAGE
-
monomer
1 * 40700, calculated from sequence, 1 * 40000, SDS-PAGE, His-tagged recombinant protein
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
H282G
by site-directed mutagenesis
H306A
-
very low activity, substrate is bound to ferrous heme
H282G
-
by site-directed mutagenesis
-
H306A
-
very low activity, substrate is bound to ferrous heme
-
additional information
the H282G mutant has no enzymatic activity, the enzymatic activity is rescued by imidazole or pyridine derivatives that act as exogenous proximal ligand
additional information
-
the H282G mutant has no enzymatic activity, the enzymatic activity is rescued by imidazole or pyridine derivatives that act as exogenous proximal ligand
additional information
-
the H282G mutant has no enzymatic activity, the enzymatic activity is rescued by imidazole or pyridine derivatives that act as exogenous proximal ligand
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
10
-
denaturation above
659505
6
-
denaturation below
659505
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
by Co2+-charged metal-ion-chelating Talon column chromatography
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
amino-terminal His6-tagged H282G OxdB expressed in Escherichia coli
expressed in Escherichia coli C41 (DE3) cells
expression in Escherichia coli
overexpression in Escherichia coli
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
synthesis
-
high yield synthesis of 3-phenylpropionitrile from unpurified (E/Z)-3-phenylpropionaldoxime, which is spontaneously formed from 3-phenlypropionaldehyde and hydroxylamine in a butyl acetate/water biphasic system, production of further nitriles from their corresponding aldoximes
synthesis
-
production of enzyme by expression in Escherichia coli and Bacillus subtilis, at 37°C, yield of mainly inactive inclusion bodies, at 30°C, enzyme is largely soluble and active. Enhancement of production by increasing the volume of culture medium
synthesis
-
high yield synthesis of 3-phenylpropionitrile from unpurified (E/Z)-3-phenylpropionaldoxime, which is spontaneously formed from 3-phenlypropionaldehyde and hydroxylamine in a butyl acetate/water biphasic system, production of further nitriles from their corresponding aldoximes
-
synthesis
-
production of enzyme by expression in Escherichia coli and Bacillus subtilis, at 37°C, yield of mainly inactive inclusion bodies, at 30°C, enzyme is largely soluble and active. Enhancement of production by increasing the volume of culture medium
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Kato, Y.; Nakamura, K.; Sakiyama, H.; Mayhew, S.G.; Asano, Y.
Novel heme-containing lyase, phenylacetaldoxime dehydratase from Bacillus sp. strain OxB-1: purification, characterization, and molecular cloning of the gene
Biochemistry
39
800-809
2000
Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) OxB-1
brenda
Xie, S.X.; Kato, Y.; Asano, Y.
High yield synthesis of nitriles by a new enzyme, phenylacetaldoxime dehydratase, from Bacillus sp. strain OxB-1
Biosci. Biotechnol. Biochem.
65
2666-2672
2001
Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) OxB-1
brenda
Asano, Y.; Kato, Y.
Z-phenylacetaldoxime degradation by a novel aldoxime dehydratase from Bacillus sp. strain OxB-1
FEMS Microbiol. Lett.
158
185-190
1998
Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) OxB-1
-
brenda
Kobayashi, K.; Yoshioka, S.; Kato, Y.; Asano, Y.; Aono, S.
Regulation of aldoxime dehydratase activity by redox-dependent change in the coordination structure of the aldoxime-heme complex
J. Biol. Chem.
280
5486-5490
2005
Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) OxB-1
brenda
Kato, Y.; Asano, Y.
High-level expression of a novel FMN-dependent heme-containing lyase, phenylacetaldoxime dehydratase of Bacillus sp. strain OxB-1, in heterologous hosts
Protein Expr. Purif.
28
131-139
2003
Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) OxB-1
brenda
Kato, Y.; Asano, Y.
Purification and characterization of aldoxime dehydratase of the head blight fungus, Fusarium graminearum
Biosci. Biotechnol. Biochem.
69
2254-2257
2005
Fusarium graminearum (Q2WG72), Fusarium graminearum, Fusarium graminearum MAFF305135 (Q2WG72), Fusarium graminearum MAFF305135
brenda
Kobayashi, K.; Pal, B.; Yoshioka, S.; Kato, Y.; Asano, Y.; Kitagawa, T.; Aono, S.
Spectroscopic and substrate binding properties of heme-containing aldoxime dehydratases, OxdB and OxdRE
J. Inorg. Biochem.
100
1069-1074
2006
Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) OxB-1, Rhodococcus sp.
brenda
Kobayashi, K.; Kubo, M.; Yoshioka, S.; Kitagawa, T.; Kato, Y.; Asano, Y.; Aono, S.
Systematic regulation of the enzymatic activity of phenylacetaldoxime dehydratase by exogenous ligands
Chembiochem
7
2004-2009
2006
Bacillus sp. (in: Bacteria) (P82604), Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) OxB-1 (P82604)
brenda
Miki, Y.; Asano, Y.
Construction of the biosynthetic pathway for the cyanide-free production of phenylacetonitrile in Escherichia coli utilizing plant cytochrome P450 79A2 and bacterial aldoxime dehydratase
Appl. Environ. Microbiol.
80
6828-6836
2014
Bacillus sp. (in: Bacteria) (P82604), Bacillus sp. (in: Bacteria) OxB-1 (P82604)
brenda
Raedisch, R.; Chmatal, M.; Rucka, L.; Novotny, P.; Petraskova, L.; Halada, P.; Kotik, M.; Patek, M.; Martinkova, L.
Overproduction and characterization of the first enzyme of a new aldoxime dehydratase family in Bradyrhizobium sp.
Int. J. Biol. Macromol.
115
746-753
2018
Bradyrhizobium sp. LTSPM299 (A0A0D7Q864)
brenda
Select items on the left to see more content.
html completed