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(1E)-2-(1,3-benzodioxol-5-yl)-N-hydroxypropan-1-imine
(2S)-2-(1,3-benzodioxol-5-yl)propanenitrile + H2O
(1E)-N-hydroxy-2,6-dimethylhept-5-en-1-imine
(2S)-2,6-dimethylhept-5-en-1-imine + H2O
(1E)-N-hydroxy-2-(thiophen-2-yl)propan-1-imine
(2R)-2-(thiophen-2-yl)propanenitrile + H2O
(1E)-N-hydroxy-2-phenylpropan-1-imine
(2S)-2-phenylpropanenitrile + H2O
(1E)-N-hydroxybutan-1-imine
butanenitrile + H2O
(1E)-N-hydroxyethanimine
acetonitrile + H2O
-
-
-
-
?
(E)-4-chlorobenzaldoxime
?
-
0.331% activity in the presence of Na2S compared to (Z)-phenylacetaldehyde oxime
-
-
?
(E)-4-tolualdoxime
?
-
0.488% activity in the presence of Na2S compared to (Z)-phenylacetaldehyde oxime
-
-
?
(E)-acetaldoxime
?
-
-
-
-
?
(E)-benzaldoxime
?
-
1.92% activity in the presence of Na2S compared to (Z)-phenylacetaldehyde oxime
-
-
?
(E)-furfurylaldoxime
?
-
0.504% activity in the presence of Na2S compared to (Z)-phenylacetaldehyde oxime
-
-
?
(E)-pyridine-3-aldoxime
?
-
0.535% activity in the presence of Na2S compared to (Z)-phenylacetaldehyde oxime
-
-
?
(E)-pyridine-3-aldoxime
pyridine-3-nitrile + H2O
not Z-form, poor substrate, 0.78% of the activity with (E/Z)-cyclohexanecarboxaldehyde oxime
-
?
(E)-thiophene-2-acetaldoxime
?
-
26.3% activity in the presence of Na2S compared to (Z)-phenylacetaldehyde oxime
-
-
?
(E)-thiophene-2-carboxaldoxime
?
-
3.37% activity in the presence of Na2S compared to (Z)-phenylacetaldehyde oxime
-
-
?
(E/Z)-2-phenylpropionaldoxime
(E/Z)-2-phenylpropiononitrile + H2O
-
49.8% activity in the presence of Na2S compared to (Z)-phenylacetaldehyde oxime
-
-
?
(E/Z)-2-phenylpropionaldoxime
2-phenylpropionitrile + H2O
(E/Z)-2-phenylpropionaldoxime
2-phenylpropiononitrile + H2O
5.23% of the activity with (E/Z)-cyclohexanecarboxaldehyde oxime
-
?
(E/Z)-3-phenylpropionaldoxime
3-phenylpropionitrile + H2O
-
-
-
?
(E/Z)-4-phenybutyraldoxime
4-phenybutyrnitrile + H2O
-
-
-
?
(E/Z)-4-phenylbutyraldoxime
phenylbutyronitrile + H2O
-
29.1% activity in the presence of Na2S compared to (Z)-phenylacetaldehyde oxime
-
-
?
(E/Z)-acetaldoxime
acetonitrile + H2O
(E/Z)-cinnamaldehyde oxime
?
-
4.28% activity in the presence of Na2S compared to (Z)-phenylacetaldehyde oxime
-
-
?
(E/Z)-cyclohexanecarboxaldehyde oxime
?
(E/Z)-cyclohexanecarboxaldehyde oxime
cyclohexanenitrile + H2O
-
-
-
?
(E/Z)-indoleacetaldoxime
indoleacetonitrile + H2O
(E/Z)-isobutyraldoxime
?
-
89.6% activity in the presence of Na2S compared to (Z)-phenylacetaldehyde oxime
-
-
?
(E/Z)-isobutyraldoxime
isobutyrnitrile + H2O
-
-
-
?
(E/Z)-isobutyraldoxime
isobutyronitrile + H2O
26.5% of the activity with (E/Z)-cyclohexanecarboxaldehyde oxime
-
?
(E/Z)-isocapronaldoxime
isocapronitrile + H2O
-
48.7% activity in the presence of Na2S compared to (Z)-phenylacetaldehyde oxime
-
-
?
(E/Z)-isocapronaldoxime
isocaprononitrile + H2O
(E/Z)-isovaleraldoxime
isovalernitrile + H2O
-
-
-
?
(E/Z)-isovaleraldoxime
isovaleronitrile + H2O
(E/Z)-mandelaldoxime
mandeloacetonitrile + H2O
-
11.7% activity in the presence of Na2S compared to (Z)-phenylacetaldehyde oxime
-
-
?
(E/Z)-mandelaldoxime
mandelonitrile + H2O
3.09% of the activity with (E/Z)-cyclohexanecarboxaldehyde oxime
-
?
(E/Z)-n-butyraldoxime
n-butyrnitrile + H2O
-
-
-
?
(E/Z)-n-butyraldoxime
n-butyronitrile + H2O
(E/Z)-n-capronaldoxime
n-capronnitrile + H2O
-
-
-
?
(E/Z)-n-capronaldoxime
n-caprononitrile + H2O
(E/Z)-n-valeraldoxime
n-valernitrile + H2O
-
-
-
?
(E/Z)-n-valeraldoxime
n-valeronitrile + H2O
(E/Z)-propionaldoxime
propionitrile + H2O
(E/Z)-propionaldoxime
propiononitrile + H2O
7.76% of the activity with (E/Z)-cyclohexanecarboxaldehyde oxime
-
?
(E/Z)-pyridine-2-aldoxime
pyridine-2-nitrile + H2O
poor substrate
-
?
(Z)-1-(cyclohex-3-en-1-yl)-N-hydroxymethanimine
(1S)-cyclohex-3-ene-1-carbonitrile + H2O
-
54% conversion, 4% ee (+)
-
-
?
(Z)-3-phenylpropionaldoxime
3-phenylpropiononitrile
-
69.6% activity in the presence of Na2S compared to (Z)-phenylacetaldehyde oxime
-
-
?
(Z)-3-phenylpropionaldoxime
3-phenylpropiononitrile + H2O
(Z)-4-chlorophenylacetaldoxime
4-chlorophenylacetonitrile + H2O
-
3.39% activity in the presence of Na2S compared to (Z)-phenylacetaldehyde oxime
-
-
?
(Z)-acetaldoxime
?
-
preferred substrate
-
-
?
(Z)-naphthoacetaldoxime
naphthoacetonitrile + H2O
-
2.71% activity in the presence of Na2S compared to (Z)-phenylacetaldehyde oxime
-
-
?
(Z)-phenylacetaldehyde oxime
phenylacetonitrile + H2O
-
100% activity in the presence of Na2S
-
-
?
(Z)-phenylacetaldoxime
phenylacetonitrile + H2O
5-nitro-1,2-benzoxazole
2-hydroxy-5-nitrobenzonitrile
aliphatic aldoxime
aliphatic nitrile + H2O
alkylaldoxime
alkylnitrile + H2O
an aliphatic aldoxime
an aliphatic nitrile + H2O
butyraldoxime
butyronitrile + H2O
n-butyraldoxime
n-butyronitrile + H2O
propionaldoxime
propionitrile + H2O
-
-
-
?
additional information
?
-
(1E)-2-(1,3-benzodioxol-5-yl)-N-hydroxypropan-1-imine
(2S)-2-(1,3-benzodioxol-5-yl)propanenitrile + H2O
-
17% conversion, 56% ee (S)
-
-
?
(1E)-2-(1,3-benzodioxol-5-yl)-N-hydroxypropan-1-imine
(2S)-2-(1,3-benzodioxol-5-yl)propanenitrile + H2O
-
17% conversion, 56% ee (S)
-
-
?
(1E)-N-hydroxy-2,6-dimethylhept-5-en-1-imine
(2S)-2,6-dimethylhept-5-en-1-imine + H2O
-
38% conversion, 43% ee (+)
-
-
?
(1E)-N-hydroxy-2,6-dimethylhept-5-en-1-imine
(2S)-2,6-dimethylhept-5-en-1-imine + H2O
-
38% conversion, 43% ee (+)
-
-
?
(1E)-N-hydroxy-2-(thiophen-2-yl)propan-1-imine
(2R)-2-(thiophen-2-yl)propanenitrile + H2O
-
18% conversion, 35% ee (-)
-
-
?
(1E)-N-hydroxy-2-(thiophen-2-yl)propan-1-imine
(2R)-2-(thiophen-2-yl)propanenitrile + H2O
-
18% conversion, 35% ee (-)
-
-
?
(1E)-N-hydroxy-2-phenylpropan-1-imine
(2S)-2-phenylpropanenitrile + H2O
-
26% conversion, 91% ee (S)
-
-
?
(1E)-N-hydroxy-2-phenylpropan-1-imine
(2S)-2-phenylpropanenitrile + H2O
-
26% conversion, 91% ee (S)
-
-
?
(1E)-N-hydroxybutan-1-imine
butanenitrile + H2O
-
-
-
-
?
(1E)-N-hydroxybutan-1-imine
butanenitrile + H2O
-
-
-
-
?
(E/Z)-2-phenylpropionaldoxime
2-phenylpropionitrile + H2O
-
-
-
?
(E/Z)-2-phenylpropionaldoxime
2-phenylpropionitrile + H2O
-
-
-
?
(E/Z)-acetaldoxime
acetonitrile + H2O
-
-
?
(E/Z)-acetaldoxime
acetonitrile + H2O
-
-
?
(E/Z)-cyclohexanecarboxaldehyde oxime
?
best substrate
-
?
(E/Z)-cyclohexanecarboxaldehyde oxime
?
best substrate
-
?
(E/Z)-cyclohexanecarboxaldehyde oxime
?
-
157% activity in the presence of Na2S compared to (Z)-phenylacetaldehyde oxime
-
-
?
(E/Z)-indoleacetaldoxime
indoleacetonitrile + H2O
7.29% of the activity with (E/Z)-cyclohexanecarboxaldehyde oxime
-
?
(E/Z)-indoleacetaldoxime
indoleacetonitrile + H2O
-
41.7% activity in the presence of Na2S compared to (Z)-phenylacetaldehyde oxime
-
-
?
(E/Z)-isocapronaldoxime
isocaprononitrile + H2O
-
-
-
?
(E/Z)-isocapronaldoxime
isocaprononitrile + H2O
-
-
-
?
(E/Z)-isocapronaldoxime
isocaprononitrile + H2O
88.3% of the activity with (E/Z)-cyclohexanecarboxaldehyde oxime
-
?
(E/Z)-isovaleraldoxime
isovaleronitrile + H2O
58.6% of the activity with (E/Z)-cyclohexanecarboxaldehyde oxime
-
?
(E/Z)-isovaleraldoxime
isovaleronitrile + H2O
-
120% activity in the presence of Na2S compared to (Z)-phenylacetaldehyde oxime
-
-
?
(E/Z)-n-butyraldoxime
n-butyronitrile + H2O
-
-
-
?
(E/Z)-n-butyraldoxime
n-butyronitrile + H2O
best substrate, accepts both the E- and the Z-forms of butyraldoxime as substrates
butyronitrile does not act as substrate
?
(E/Z)-n-butyraldoxime
n-butyronitrile + H2O
-
-
-
?
(E/Z)-n-butyraldoxime
n-butyronitrile + H2O
best substrate, accepts both the E- and the Z-forms of butyraldoxime as substrates
butyronitrile does not act as substrate
?
(E/Z)-n-butyraldoxime
n-butyronitrile + H2O
48.9% of the activity with (E/Z)-cyclohexanecarboxaldehyde oxime
-
?
(E/Z)-n-butyraldoxime
n-butyronitrile + H2O
48.9% of the activity with (E/Z)-cyclohexanecarboxaldehyde oxime
-
?
(E/Z)-n-butyraldoxime
n-butyronitrile + H2O
-
100% activity in the presence of Na2S compared to (Z)-phenylacetaldehyde oxime
-
-
?
(E/Z)-n-capronaldoxime
n-caprononitrile + H2O
64.2% of the activity with (E/Z)-cyclohexanecarboxaldehyde oxime
-
?
(E/Z)-n-capronaldoxime
n-caprononitrile + H2O
-
85.5% activity in the presence of Na2S compared to (Z)-phenylacetaldehyde oxime
-
-
?
(E/Z)-n-valeraldoxime
n-valeronitrile + H2O
39.3% of the activity with (E/Z)-cyclohexanecarboxaldehyde oxime
-
?
(E/Z)-n-valeraldoxime
n-valeronitrile + H2O
39.3% of the activity with (E/Z)-cyclohexanecarboxaldehyde oxime
-
?
(E/Z)-n-valeraldoxime
n-valeronitrile + H2O
-
68.3% activity in the presence of Na2S compared to (Z)-phenylacetaldehyde oxime
-
-
?
(E/Z)-propionaldoxime
propionitrile + H2O
-
-
-
?
(E/Z)-propionaldoxime
propionitrile + H2O
-
-
-
?
(E/Z)-propionaldoxime
propionitrile + H2O
-
87.7% activity in the presence of Na2S compared to (Z)-phenylacetaldehyde oxime
-
-
?
(Z)-3-phenylpropionaldoxime
3-phenylpropiononitrile + H2O
-
-
-
?
(Z)-3-phenylpropionaldoxime
3-phenylpropiononitrile + H2O
-
-
-
?
(Z)-3-phenylpropionaldoxime
3-phenylpropiononitrile + H2O
67.3% of the activity with (E/Z)-cyclohexanecarboxaldehyde oxime
-
?
(Z)-phenylacetaldoxime
phenylacetonitrile + H2O
-
-
-
?
(Z)-phenylacetaldoxime
phenylacetonitrile + H2O
-
-
-
?
(Z)-phenylacetaldoxime
phenylacetonitrile + H2O
-
-
-
?
(Z)-phenylacetaldoxime
phenylacetonitrile + H2O
26.6% of the activity with (E/Z)-cyclohexanecarboxaldehyde oxime
-
?
(Z)-phenylacetaldoxime
phenylacetonitrile + H2O
26.6% of the activity with (E/Z)-cyclohexanecarboxaldehyde oxime
-
?
5-nitro-1,2-benzoxazole
2-hydroxy-5-nitrobenzonitrile
-
-
-
?
5-nitro-1,2-benzoxazole
2-hydroxy-5-nitrobenzonitrile
-
-
-
?
5-nitro-1,2-benzoxazole
2-hydroxy-5-nitrobenzonitrile
-
-
-
?
aldoxime
nitrile + H2O
wide range of substrates, aliphatic aldoximes are more effective substrates than arylalkyl aldoximes, aromatic aldoximes are also dehydrated
-
?
aldoxime
nitrile + H2O
wide range of substrates, aliphatic aldoximes are more effective substrates than arylalkyl aldoximes, aromatic aldoximes are also dehydrated
-
?
aliphatic aldoxime
aliphatic nitrile + H2O
strong preference of aliphatic aldoximes over aromatic aldoximes
-
?
aliphatic aldoxime
aliphatic nitrile + H2O
strong preference of aliphatic aldoximes over aromatic aldoximes
-
?
alkylaldoxime
alkylnitrile + H2O
-
-
-
?
alkylaldoxime
alkylnitrile + H2O
responsible for the metabolism of alkylaldoxime
-
?
an aliphatic aldoxime
an aliphatic nitrile + H2O
-
-
-
-
?
an aliphatic aldoxime
an aliphatic nitrile + H2O
-
-
-
-
?
an aliphatic aldoxime
an aliphatic nitrile + H2O
-
-
-
?
an aliphatic aldoxime
an aliphatic nitrile + H2O
-
-
-
-
?
an aliphatic aldoxime
an aliphatic nitrile + H2O
-
-
-
?
an aliphatic aldoxime
an aliphatic nitrile + H2O
-
-
-
-
?
an aliphatic aldoxime
an aliphatic nitrile + H2O
-
-
-
?
an aliphatic aldoxime
an aliphatic nitrile + H2O
-
-
-
?
an aliphatic aldoxime
an aliphatic nitrile + H2O
-
-
-
?
an aliphatic aldoxime
an aliphatic nitrile + H2O
-
-
-
-
?
an aliphatic aldoxime
an aliphatic nitrile + H2O
-
the enzyme preferentially acts on aliphatic-type substrates
-
-
?
butyraldoxime
butyronitrile + H2O
-
-
-
-
?
butyraldoxime
butyronitrile + H2O
-
-
addition of 200 mM butyraldoxime to ferrous OxdA yields a longlived OxdA-substrate complex, named OS-II
-
?
butyraldoxime
butyronitrile + H2O
-
the substrate binds to heme forming a hexa-coordinate low-spin heme
-
-
?
butyraldoxime
butyronitrile + H2O
-
-
addition of 200 mM butyraldoxime to ferrous OxdA yields a longlived OxdA-substrate complex, named OS-II
-
?
butyraldoxime
butyronitrile + H2O
-
the substrate binds to heme forming a hexa-coordinate low-spin heme
-
-
?
butyraldoxime
butyronitrile + H2O
-
-
-
-
?
butyraldoxime
butyronitrile + H2O
-
-
-
?
n-butyraldoxime
n-butyronitrile + H2O
-
reaction intermediate of the heme-containing enzyme with a highly oxidized heme that is formed concomitantly upon direct binding of the substrate, heme directly activates the organic substrate
-
-
?
n-butyraldoxime
n-butyronitrile + H2O
-
reaction intermediate of the heme-containing enzyme with a highly oxidized heme that is formed concomitantly upon direct binding of the substrate, heme directly activates the organic substrate
-
-
?
additional information
?
-
-
not: butyronitrile, aromatic aldoximes, such as benzaldoxime, isonitrosoacetophenone, and pyridine-4-aldoxime
-
?
additional information
?
-
not: butyronitrile, aromatic aldoximes, such as benzaldoxime, isonitrosoacetophenone, and pyridine-4-aldoxime
-
?
additional information
?
-
-
involved in carbon-nitrogen triple bond synthesis, responsible for the metabolism of aldoxime in vivo
-
?
additional information
?
-
involved in carbon-nitrogen triple bond synthesis, responsible for the metabolism of aldoxime in vivo
-
?
additional information
?
-
enzyme additionally shows catalase activity, reaction of EC 1.11.1.6, and peroxidase activity
-
-
?
additional information
?
-
-
not: butyronitrile, aromatic aldoximes, such as benzaldoxime, isonitrosoacetophenone, and pyridine-4-aldoxime
-
?
additional information
?
-
not: butyronitrile, aromatic aldoximes, such as benzaldoxime, isonitrosoacetophenone, and pyridine-4-aldoxime
-
?
additional information
?
-
-
involved in carbon-nitrogen triple bond synthesis, responsible for the metabolism of aldoxime in vivo
-
?
additional information
?
-
involved in carbon-nitrogen triple bond synthesis, responsible for the metabolism of aldoxime in vivo
-
?
additional information
?
-
-
the following compounds are inert as substrates: ((E/Z))-diphenylacetaldoxime, ((E/Z))-4-hydroxyphenylacetaldoxime, (E)-1-naphthoaldoxime, (E)-anisaldoxime, (E)-quinolin(E)-2-carboxaldehyde oxime, (E)-terephthalaldehyde oxime, (E)-isophthalaldehyde oxime, (E)-pyrazinecarboxaldoxime, (E)-indol(E)-3-carboxaldehyde oxime, (Z)-crotonaldoxime, ((E/Z))-methacrylaldoxime, ((E/Z))-O-benzylphenylacetaldehyde oxime, (E)-phenylacetaldehyde oxime hydrazone, ((E/Z))-O-acetyl-phenylacetaldehyde oxime, ((E/Z))-phenylacetone oxime and ((E/Z))-acetophenone oxime
-
-
-
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reducing reagent
requirement, activates
-
2-mercaptoethanol
activates, (Z)-phenylacetaldoxime dehydration, 1 mM, 2.13fold
2-mercaptoethanol
-
the enzyme activity is enhanced 1.8fold by 1 mM
cysteamine
activates, (Z)-phenylacetaldoxime dehydration, 1 mM, 3.93fold
cysteamine
-
the enzyme activity is enhanced 2.3fold by 1 mM
duroquinone
activates
duroquinone
-
the enzyme activity is increased 6.7fold in the absence of Na2S
FAD
1 mM, 1.2fold activation in presence of Na2S, 4.5fold in absence of Na2S
FAD
-
the enzyme activity is enhanced 3fold by 1 mM
FMN
1 mM, 1.7fold activation in presence of Na2S, 2.4fold in absence of Na2S
FMN
-
the enzyme activity is enhanced 7.2fold by 1 mM
L-cysteine
activates, (Z)-phenylacetaldoxime dehydration, 1 mM, 2.39fold
L-cysteine
-
the enzyme activity is enhanced 2.4fold by 1 mM
Na2S
activates, (Z)-phenylacetaldoxime dehydration, 1 mM, 8.35fold
Na2S
-
the enzyme activity is enhanced 4.5fold by 1 mM
Na2S2O4
requirement of a reducing agent for activity
Na2S2O4
activates, (Z)-phenylacetaldoxime dehydration, 1 mM, 8.13fold
Na2S2O4
-
the enzyme activity is enhanced 2.3fold by 1 mM
Na2S2O5
activates, (Z)-phenylacetaldoxime dehydration, 1 mM, 5.84fold
Na2S2O5
-
the enzyme activity is enhanced 13.8fold by 1 mM
Na2SO3
activates, (Z)-phenylacetaldoxime dehydration, 1 mM, 7.51fold
Na2SO3
-
the enzyme activity is enhanced 5.4fold by 1 mM
riboflavin
1 mM, 1.1fold activation in presence of Na2S, 4.2fold in absence of Na2S
riboflavin
-
the enzyme activity is enhanced 3.4fold by 1 mM
thioglycerol
activates, (Z)-phenylacetaldoxime dehydration, 1 mM, 4.06fold
thioglycerol
-
the enzyme activity is enhanced 3.5fold by 1 mM
vitamin K3
activates
vitamin K3
-
the enzyme activity is increased 23fold in the presence of Na2S
additional information
not activated by NaHSO3, Na2SO4, NaHSO4 or Na2S2O7
-
additional information
-
the activity is not increased by the additions of NaHSO3, Na2SO4, NaHSO4or Na2S2O7. The following coenzymes do not affect the reaction: pantothenate, phosphoenolpyruvate, NaF, pyridoxal, dehydroascorbate, glutathione, glutathione disulfide, NAD(P)(H), D-glucose 6-phosphate, glutathione disulfide, dehydroascorbic acid, CoA-SH, AXP, GXP, and IXP
-
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F289A
about 45% of wild-type activity
H282A
about 5% of wild-type activity
H306A
about 3% of wild-type activity
L128A
about 30% of wild-type activity
Q204A
activity similar to wild-type
T202A
about 20% of wild-type activity in absence, 50% in presence of dithionite
E143A
the mutant shows about wild type enzyme activity
E143A/R178A
the mutant shows 29.4% activity compared to the wild type enzyme
H320D
mutant shows increased catalase and peroxidase activity. The kcat value for H2O2 is 30times higher than that of wild-type, and the peroxidase activity is dozens of times higher
H338A
-
the heme content and CD spectra in the far-UV region are almost identical to that of wild-type enzyme
N279A
the mutant shows 53.1% activity compared to the wild type enzyme
Q221A
the mutant shows about wild type enzyme activity
R178A
the mutant exhibits 19.1% of wild type activity and 1.62% of wild type heme content
S174A
the mutant shows about wild type enzyme activity
S219A
the mutant has completely lost activity despite unaffected heme content
S219C
the mutant shows 2.01% activity compared to the wild type enzyme
S219T
the mutant shows 26.1% activity compared to the wild type enzyme
Y234A
the mutant shows 170% activity compared to the wild type enzyme
E143A
-
the mutant shows about wild type enzyme activity
-
H296A
-
the mutant shows 141% activity compared to the wild type enzyme
-
S174A
-
the mutant shows about wild type enzyme activity
-
E143Q
loss in enzymatic activity, 14% of the wild-type
F306A
loss in enzymatic activity, 33% of the wild-type
H320A
loss in enzymatic activity, 11% of the wild-type
R178Q
loss in enzymatic activity, 36% of the wild-type
S219A
loss in enzymatic activity, 23% of the wild-type
H299A
-
the mutation leads to the loss of the ability to bind heme, thus becoming inactive
H169A
-
the heme content and CD spectra in the far-UV region are almost identical to that of wild-type enzyme
H169A
the mutant shows 123% activity compared to the wild type enzyme
H296A
-
the heme content and CD spectra in the far-UV region are almost identical to that of wild-type enzyme
H296A
the mutant shows 141% activity compared to the wild type enzyme
H299A
-
mutant is unable to bind heme
H299A
-
the heme content and CD spectra in the far-UV region are almost identical to that of wild-type enzyme
H320A
-
mutation does not affect the overall structure of OxdA but causes loss of its ability of carbon-nitrogen triple bond synthesis and a lower shift of the Fe-C stretching band in the Raman spectrum for the CO-bound form
H320A
-
the heme content and CD spectra in the far-UV region are almost identical to that of wild-type enzyme
H320A
the mutant shows 0.137% activity compared to the wild type enzyme
H169A
-
the heme content and CD spectra in the far-UV region are almost identical to that of wild-type enzyme
-
H169A
-
the mutant shows 123% activity compared to the wild type enzyme
-
H299A
-
mutant is unable to bind heme
-
H299A
-
the heme content and CD spectra in the far-UV region are almost identical to that of wild-type enzyme
-
H320A
-
mutation does not affect the overall structure of OxdA but causes loss of its ability of carbon-nitrogen triple bond synthesis and a lower shift of the Fe-C stretching band in the Raman spectrum for the CO-bound form
-
H320A
-
the heme content and CD spectra in the far-UV region are almost identical to that of wild-type enzyme
-
H320A
-
the mutant shows 0.137% activity compared to the wild type enzyme
-
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Oinuma, K-I.; Hashimoto, Y.; Konishi, K.; Goda, M.; Noguchi, T.; Higashibata, H.; Kobayashi, M.
Novel aldoxime dehydratase involved in carbon-nitrogen triple bond synthesis of Pseudomonas chlororaphis B23: Sequencing, gene expression, purification and characterization
J. Biol. Chem.
278
29600-29608
2003
Pseudomonas chlororaphis, Pseudomonas chlororaphis (Q7WSJ4), Pseudomonas chlororaphis B23, Pseudomonas chlororaphis B23 (Q7WSJ4)
brenda
Xie, S.X.; Kato, Y.; Komeda, H.; Yoshida, S.; Asano, Y.
A gene cluster responsible for alkylaldoxime metabolism coexisting with nitrile hydratase and amidase in Rhodococcus globerulus A-4
Biochemistry
42
12056-12066
2003
Rhodococcus globerulus (Q76EV4), Rhodococcus globerulus A-4 (Q76EV4), Rhodococcus globerulus A-4
brenda
Oinuma, K.; Ohta, T.; Konishi, K.; Hashimoto, Y.; Higashibata, H.; Kitagawa, T.; Kobayashi, M.
Heme environment in aldoxime dehydratase involved in carbon-nitrogen triple bond synthesis
FEBS Lett.
568
44-48
2004
Pseudomonas chlororaphis, Pseudomonas chlororaphis B23
brenda
Oinuma, K.; Kumita, H.; Ohta, T.; Konishi, K.; Hashimoto, Y.; Higashibata, H.; Kitagawa, T.; Shiro, Y.; Kobayashi, M.
Stopped-flow spectrophotometric and resonance Raman analyses of aldoxime dehydratase involved in carbon-nitrogen triple bond synthesis
FEBS Lett.
579
1394-1398
2005
Pseudomonas chlororaphis, Pseudomonas chlororaphis B23
brenda
Konishi, K.; Ishida, K.; Oinuma, K.; Ohta, T.; Hashimoto, Y.; Higashibata, H.; Kitagawa, T.; Kobayashi, M.
Identification of crucial histidines involved in carbon-nitrogen triple bond synthesis by aldoxime dehydratase
J. Biol. Chem.
279
47619-47625
2004
Pseudomonas chlororaphis, Pseudomonas chlororaphis B23
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), Rhodococcus sp., Bacillus sp. (in: Bacteria) OxB-1
brenda
Konishi, K.; Ohta, T.; Oinuma, K.; Hashimoto, Y.; Kitagawa, T.; Kobayashi, M.
Discovery of a reaction intermediate of aliphatic aldoxime dehydratase involving heme as an active center
Proc. Natl. Acad. Sci. USA
103
564-568
2006
Pseudomonas chlororaphis, Pseudomonas chlororaphis B23
brenda
Kato, Y.; Asano, Y.
Molecular and enzymatic analysis of the "aldoxime-nitrile pathway" in the glutaronitrile degrader Pseudomonas sp. K-9
Appl. Microbiol. Biotechnol.
70
92-101
2006
Pseudomonas sp. (Q4W7T3), Pseudomonas sp., Pseudomonas sp. K-9 (Q4W7T3)
brenda
Sawai, H.; Sugimoto, H.; Kato, Y.; Asano, Y.; Shiro, Y.; Aono, S.
X-ray crystal structure of michaelis complex of aldoxime dehydratase
J. Biol. Chem.
284
32089-32096
2009
Rhodococcus erythropolis (Q76K71)
brenda
Pinakoulaki, E.; Koutsoupakis, C.; Sawai, H.; Pavlou, A.; Kato, Y.; Asano, Y.; Aono, S.
Aldoxime dehydratase: probing the heme environment involved in the synthesis of the carbon-nitrogen triple bond
J. Phys. Chem. B
115
13012-13018
2011
Rhodococcus sp.
brenda
Pan, X.L.; Cui, F.C.; Liu, W.; Liu, J.Y.
QM/MM study on the catalytic mechanism of heme-containing aliphatic aldoxime dehydratase
J. Phys. Chem. B
116
5689-5693
2012
Pseudomonas chlororaphis (Q7WSJ4), Pseudomonas chlororaphis B23 (Q7WSJ4)
brenda
Liao, R.Z.; Thiel, W.
Why is the oxidation state of iron crucial for the activity of heme-dependent aldoxime dehydratase? A QM/MM study
J. Phys. Chem. B
116
9396-9408
2012
Rhodococcus sp.
brenda
Nomura, J.; Hashimoto, H.; Ohta, T.; Hashimoto, Y.; Wada, K.; Naruta, Y.; Oinuma, K.; Kobayashi, M.
Crystal structure of aldoxime dehydratase and its catalytic mechanism involved in carbon-nitrogen triple-bond synthesis
Proc. Natl. Acad. Sci. USA
110
2810-2815
2013
Pseudomonas chlororaphis (Q7WSJ4), Pseudomonas chlororaphis B23 (Q7WSJ4)
brenda
Miao, Y.; Metzner, R.; Asano, Y.
Kemp elimination catalyzed by naturally occurring aldoxime dehydratases
ChemBioChem
18
451-454
2017
Bacillus sp. OxB-1 (A0A0A8JIJ3), Rhodococcus sp. N-771 (Q76K71), Pseudomonas chlororaphis (Q7WSJ4)
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
Pseudomonas chlororaphis (Q7WSJ4), Pseudomonas chlororaphis B23 (Q7WSJ4)
brenda
Yamada, M.; Hashimoto, Y.; Kumano, T.; Tsujimura, S.; Kobayashi, M.
New function of aldoxime dehydratase Redox catalysis and the formation of an unexpected product
PLoS ONE
12
e0175846
2017
Pseudomonas chlororaphis (Q7WSJ4)
brenda
Betke, T.; Higuchi, J.; Rommelmann, P.; Oike, K.; Nomura, T.; Kato, Y.; Asano, Y.; Groeger, H.
biocatalytic synthesis of nitriles through dehydration of aldoximes The substrate scope of aldoxime dehydratases
ChemBioChem
19
768-779
2018
Pseudomonas chlororaphis, Pseudomonas chlororaphis B23
brenda
Kato, Y.; Yoshida, S.; Xie, S.X.; Asano, Y.
Aldoxime dehydratase co-existing with nitrile hydratase and amidase in the iron-type nitrile hydratas(E)-producer Rhodococcus sp. N-771
J. Biosci. Bioeng.
97
250-259
2004
Rhodococcus sp. N-771
brenda