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Information on EC 4.99.1.7 - phenylacetaldoxime dehydratase
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4.99.1.7 phenylacetaldoxime dehydrataseIUBMB 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.
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
aldoxime dehydratase, OXD, OxdB, OxdFG, OxdRE, phenylacetaldoxime dehydratase, UP10_21065, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aldoxime dehydratase
OXD
OxdB
OxdFG
phenylacetaldoxime dehydratase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(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
-
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PATHWAY SOURCE
PATHWAYS
KEGG
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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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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
-
-
-
?
(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)-indole-3-acetaldoxime
indole-3-acetonitrile + H2O
10% of the activity with (E/Z)-phenylacetaldehyde oxime
-
-
?
(E/Z)-isocapronaldoxime
isocapronitrile + H2O
-
29.4% of activity with (Z)-phenylacetaldehyde oxime
-
-
?
(E/Z)-n-capronaldoxime
n-capronitrile + H2O
-
57.1% of activity with (Z)-phenylacetaldehyde oxime
-
-
?
(E/Z)-phenylacetaldehyde oxime
phenylacetonitrile + 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-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)-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-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)-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)-phenylacetaldoxime
phenylacetonitrile + H2O
-
-
-
?
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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
(Z)-phenylacetaldehyde oxime
phenylacetonitrile + H2O
-
-
-
?
(Z)-phenylacetaldehyde oxime
phenylacetonitrile + H2O
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
up to 5fold enhancement of activity with FMN under anaerobic conditions
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Dehydration
Regulation of aldoxime dehydratase activity by redox-dependent change in the coordination structure of the aldoxime-heme complex.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.03
(Z)-phenylacetaldehyde oxime
-
pH.0, 30°C, aerobic conditions
0.031
(Z)-phenylacetaldehyde oxime
-
pH.0, 30°C, anaerobic conditions
0.31
(Z)-phenylacetaldehyde oxime
-
pH.0, 30°C, aerobic conditions, Na2SO3 substitutes for FMN
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
0.76
(Z)-phenylacetaldoxime
H282G mutant in the presence of imidazole
0.78
(Z)-phenylacetaldoxime
H282G mutant in the presence of 1-methylimidazole
1.1
(Z)-phenylacetaldoxime
H282G mutant in the presence of 2-methylimidazole
1.64
(Z)-phenylacetaldoxime
H282G mutant in the presence of 4-methoxypyridine
2.52
(Z)-phenylacetaldoxime
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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme expression in Escherichia coli and Bacillus subtilis
-
-
brenda
enzyme expression in Escherichia coli and Bacillus subtilis
-
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A454G6H4_PSESF
293
0
32752
TrEMBL
-
C6WDR0_ACTMD
Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU 3971)
343
0
37727
TrEMBL
-
F0QD95_ACIAP
Acidovorax avenae (strain ATCC 19860 / DSM 7227 / JCM 20985 / NCPPB 1011)
353
0
40033
TrEMBL
-
A7IFL4_XANP2
Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2)
347
0
39408
TrEMBL
-
A5W3Z8_PSEP1
Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1)
352
0
39977
TrEMBL
-
B1K8P0_BURCC
Burkholderia cenocepacia (strain MC0-3)
352
0
39985
TrEMBL
-
A0A2Z2NIZ7_9GAMM
340
0
37831
TrEMBL
-
A5EKU7_BRASB
Bradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182)
340
0
38026
TrEMBL
-
A5V4Y9_SPHWW
Sphingomonas wittichii (strain RW1 / DSM 6014 / JCM 10273)
343
0
38752
TrEMBL
-
B1KM99_SHEWM
Shewanella woodyi (strain ATCC 51908 / MS32)
332
0
38259
TrEMBL
-
B1Z4N0_BURA4
Burkholderia ambifaria (strain MC40-6)
350
0
39798
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
monomer
1 * 40700, calculated from sequence, 1 * 40000, SDS-PAGE, His-tagged recombinant protein
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
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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
expression in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
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
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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), Rhodococcus sp., Bacillus sp. (in: Bacteria) OxB-1
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
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