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Enzyme Nomenclature
Information on EC 4.99.1.7 - phenylacetaldoxime dehydratase
for references in articles please use BRENDA:EC4.99.1.7
Word Map on EC 4.99.1.7
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
4.99.1.7
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RECOMMENDED NAME
GeneOntology No.
phenylacetaldoxime dehydratase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(Z)-phenylacetaldehyde oxime = phenylacetonitrile + H2O
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(Z)-phenylacetaldehyde oxime = phenylacetonitrile + H2O
oxidation state of heme controls the coordination structure of a substrate-hem complex, which regulates enzyme activity
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(Z)-phenylacetaldehyde oxime = phenylacetonitrile + H2O
oxidation state of heme controls the coordination structure of a substrate-hem complex, which regulates enzyme activity
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme expression in Escherichia coli and Bacillus subtilis
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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
(E/Z)-2-phenylpropionaldoxime
(E/Z)-2-phenylpropiononitrile + H2O
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-
-
?
(E/Z)-4-phenylbutyraldoxime
(E/Z)-4-phenylbutyronitrile + H2O
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-
-
?
(E/Z)-isocapronaldoxime
isocapronitrile + H2O
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29.4% of activity with (Z)-phenylacetaldehyde oxime
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-
?
(E/Z)-n-capronaldoxime
n-capronitrile + H2O
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57.1% of activity with (Z)-phenylacetaldehyde oxime
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-
?
(E/Z)-propionaldoxime
propionitrile + H2O
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8.2% of activity with (Z)-phenylacetaldehyde oxime
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-
?
(Z)-3-phenylpropionaldoxime
phenylpropionitrile + H2O
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63% of activity with (Z)-phenylacetaldehyde oxime
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-
?
(Z)-naphthoacetaldoxime
naphthoacetonitrile + H2O
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4.5% of activity with (Z)-phenylacetaldehyde oxime
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-
?
(Z)-p-chlorophenylacetaldoxime
p-chlorophenylacetonitrile + H2O
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7.3% of activity with (Z)-phenylacetaldehyde oxime
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-
?
(Z)-p-methoxyphenylacetaldoxime
p-methoxyphenylacetonitrile + H2O
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6.8% of activity with (Z)-phenylacetaldehyde oxime
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?
Z-3-phenylpropionaldoxime
Z-3-phenylpropiononitrile + H2O
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-
-
?
(E/Z)-4-phenylbutyraldoxime
phenylbutyronitrile + H2O
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6.8% of activity with (Z)-phenylacetaldehyde oxime
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?
(E/Z)-4-phenylbutyraldoxime
phenylbutyronitrile + H2O
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6.8% of activity with (Z)-phenylacetaldehyde oxime
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-
?
(E/Z)-indoleacetaldoxime
indoleacetonitrile + H2O
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18.1% of activity with (Z)-phenylacetaldehyde oxime
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-
?
(E/Z)-indoleacetaldoxime
indoleacetonitrile + H2O
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18.1% of activity with (Z)-phenylacetaldehyde oxime
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-
?
(E/Z)-isovaleraldoxime
isovaleronitrile + H2O
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20.2% of activity with (Z)-phenylacetaldehyde oxime
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-
?
(E/Z)-isovaleraldoxime
isovaleronitrile + H2O
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20.2% of activity with (Z)-phenylacetaldehyde oxime
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-
?
(E/Z)-n-butyraldoxime
n-butyronitrile + H2O
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11% of activity with (Z)-phenylacetaldehyde oxime
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-
?
(E/Z)-n-butyraldoxime
n-butyronitrile + H2O
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11% of activity with (Z)-phenylacetaldehyde oxime
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-
?
(E/Z)-n-valeraldoxime
n-valeronitrile + H2O
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39.3% of activity with (Z)-phenylacetaldehyde oxime
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-
?
(E/Z)-n-valeraldoxime
n-valeronitrile + H2O
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39.3% of activity with (Z)-phenylacetaldehyde oxime
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?
(Z)-3-phenylpropionaldoxime
3-phenylpropionitrile + H2O
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quantitative yield of product
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?
(Z)-3-phenylpropionaldoxime
3-phenylpropionitrile + H2O
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quantitative yield of product
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?
(Z)-phenylacetaldehyde oxime
phenylacetonitrile + H2O
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?
(Z)-phenylacetaldehyde oxime
phenylacetonitrile + H2O
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?
(Z)-phenylacetaldehyde oxime
phenylacetonitrile + H2O
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?
(Z)-phenylacetaldehyde oxime
phenylacetonitrile + H2O
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?
(Z)-phenylacetaldehyde oxime
phenylacetonitrile + H2O
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?
(Z)-phenylacetaldehyde oxime
phenylacetonitrile + H2O
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?
(Z)-phenylacetaldoxime
phenylacetonitrile + H2O
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?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
(Z)-phenylacetaldehyde oxime
phenylacetonitrile + H2O
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?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
heme
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active state contains ferrous 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
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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
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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
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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up to 5fold enhancement of activity with FMN under anaerobic conditions
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.03
(Z)-phenylacetaldehyde oxime
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pH.0, 30°C, aerobic conditions
0.031
(Z)-phenylacetaldehyde oxime
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pH.0, 30°C, anaerobic conditions
0.31
(Z)-phenylacetaldehyde oxime
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pH.0, 30°C, aerobic conditions, Na2SO3 substitutes for FMN
0.38
(Z)-phenylacetaldoxime
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H282G mutant in the presence of pyridine
0.46
(Z)-phenylacetaldoxime
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H282G mutant in the presence of 4-chloropyridine
0.47
(Z)-phenylacetaldoxime
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H282G mutant in the presence of 4-methylimidazole
0.48
(Z)-phenylacetaldoxime
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H282G mutant in the presence of 4-acetylpyridine
0.67
(Z)-phenylacetaldoxime
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H282G mutant in the presence of 4-methylpyridine
0.76
(Z)-phenylacetaldoxime
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H282G mutant in the presence of imidazole
0.78
(Z)-phenylacetaldoxime
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H282G mutant in the presence of 1-methylimidazole
1.1
(Z)-phenylacetaldoxime
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H282G mutant in the presence of 2-methylimidazole
1.64
(Z)-phenylacetaldoxime
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H282G mutant in the presence of 4-methoxypyridine
2.52
(Z)-phenylacetaldoxime
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H282G mutant in the presence of 1-vinylimidazole
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by Co2+-charged metal-ion-chelating Talon column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
amino-terminal His6-tagged H282G OxdB expressed in Escherichia coli
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expression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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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
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the H282G mutant has no enzymatic activity, the enzymatic activity is rescued by imidazole or pyridine derivatives that act as exogenous proximal ligand
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
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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
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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
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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; 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
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LINKS TO OTHER DATABASES (specific for EC-Number 4.99.1.7)
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