Information on EC 4.99.1.7 - phenylacetaldoxime dehydratase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
4.99.1.7
-
RECOMMENDED NAME
GeneOntology No.
phenylacetaldoxime dehydratase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(Z)-phenylacetaldehyde oxime = phenylacetonitrile + H2O
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Cyanoamino acid metabolism
-
-
Microbial metabolism in diverse environments
-
-
NIL
-
-
prunasin and amygdalin biosynthesis
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Styrene degradation
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-
SYSTEMATIC NAME
IUBMB Comments
(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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MAFF305135
SwissProt
Manually annotated by BRENDA team
MAFF305135
SwissProt
Manually annotated by BRENDA team
N-771
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(E/Z)-2-phenylpropionaldoxime
(E/Z)-2-phenylpropiononitrile + H2O
show the reaction diagram
-
-
-
?
(E/Z)-4-phenylbutyraldoxime
(E/Z)-4-phenylbutyronitrile + H2O
show the reaction diagram
-
-
-
?
(E/Z)-4-phenylbutyraldoxime
phenylbutyronitrile + H2O
show the reaction diagram
(E/Z)-indoleacetaldoxime
(E/Z)-indoleacetonitrile + H2O
show the reaction diagram
-
-
-
?
(E/Z)-indoleacetaldoxime
indoleacetonitrile + H2O
show the reaction diagram
(E/Z)-isocapronaldoxime
isocapronitrile + H2O
show the reaction diagram
-
29.4% of activity with (Z)-phenylacetaldehyde oxime
-
-
?
(E/Z)-isovaleraldoxime
isovaleronitrile + H2O
show the reaction diagram
(E/Z)-mandelaldoxime
(E/Z)-mandeloacetonitrile + H2O
show the reaction diagram
-
-
-
?
(E/Z)-n-butyraldoxime
n-butyronitrile + H2O
show the reaction diagram
(E/Z)-n-capronaldoxime
n-capronitrile + H2O
show the reaction diagram
-
57.1% of activity with (Z)-phenylacetaldehyde oxime
-
-
?
(E/Z)-n-capronaldoxime
n-caprononitrile + H2O
show the reaction diagram
(E/Z)-n-valeraldoxime
n-valeronitrile + H2O
show the reaction diagram
(E/Z)-propionaldoxime
propionitrile + H2O
show the reaction diagram
-
8.2% of activity with (Z)-phenylacetaldehyde oxime
-
-
?
(Z)-3-phenylpropionaldoxime
3-phenylpropionitrile + H2O
show the reaction diagram
(Z)-3-phenylpropionaldoxime
phenylpropionitrile + H2O
show the reaction diagram
-
63% of activity with (Z)-phenylacetaldehyde oxime
-
-
?
(Z)-naphthoacetaldoxime
naphthoacetonitrile + H2O
show the reaction diagram
-
4.5% of activity with (Z)-phenylacetaldehyde oxime
-
-
?
(Z)-p-chlorophenylacetaldoxime
p-chlorophenylacetonitrile + H2O
show the reaction diagram
-
7.3% of activity with (Z)-phenylacetaldehyde oxime
-
-
?
(Z)-p-methoxyphenylacetaldoxime
p-methoxyphenylacetonitrile + H2O
show the reaction diagram
-
6.8% of activity with (Z)-phenylacetaldehyde oxime
-
-
?
(Z)-phenylacetaldehyde oxime
phenylacetonitrile + H2O
show the reaction diagram
(Z)-phenylacetaldoxime
phenylacetonitrile + H2O
show the reaction diagram
Z-3-phenylpropionaldoxime
Z-3-phenylpropiononitrile + H2O
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(Z)-phenylacetaldehyde oxime
phenylacetonitrile + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
-
activation
Sn2+
-
activation
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NaN3
-
activation
SO32-
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activation
sulfite
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substitutes for FMN, to a low degree
additional information
-
up to 5fold enhancement of activity with FMN under anaerobic conditions
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
activity with (Z)-phenylacetaldehyde oxime
7 - 8
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-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8
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7.8 - 8.3
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-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34100
gel filtration
40000
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native PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
His6-tagged enzyme form
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 8
stable
661363
6
-
denaturation below
659505
10
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denaturation above
659505
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
pH 7.0, stable below
45
-
stable up to
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by Co2+-charged metal-ion-chelating Talon column chromatography
partial
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H282G
by site-directed mutagenesis
H306A
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very low activity, substrate is bound to ferrous heme
H282G
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by site-directed mutagenesis
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H306A
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very low activity, substrate is bound to ferrous heme
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additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis