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Information on EC 4.8.1.3 - indoleacetaldoxime dehydratase
for references in articles please use BRENDA:EC4.8.1.3
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EC Tree 4 Lyases
4.8 Nitrogen-oxygen lyases
4.8.1 Hydro-lyases
4.8.1.3 indoleacetaldoxime dehydratase
The enzyme appears in viruses and cellular organisms
- 4.8.1.3
- camalexin
-
phytoalexin
- glucosinolates
- cyp79b2
- indole-3-acetonitrile
-
botrytis
-
necrotrophic
-
cinerea
- wrky33
-
indole-3-carboxylic
-
syringae
-
tryptophan-derived
-
defense-related
-
alternaria
-
brassicicola
showSynonyms
cyp71a13, indolyl-3-acetaldoxime dehydratase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(indol-3-yl)acetaldehyde-oxime hydro-lyase
-
-
-
-
3-indoleacetaldoxime hydro-lyase
-
-
-
-
dehydratase, indoleacetaldoxime
-
-
-
-
EC 4.2.1.29
-
-
formerly
-
EC 4.99.1.6
-
-
formerly
-
indole-3-acetaldehyde-oxime hydro-lyase
-
-
-
-
indole-3-acetaldoxime hydro-lyase
-
-
-
-
indoleacetaldoxime hydro-lyase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(indol-3-yl)acetaldehyde oxime = (indol-3-yl)acetonitrile + H2O
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
(indol-3-yl)acetaldehyde-oxime hydro-lyase [(indol-3-yl)acetonitrile-forming]
-
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CAS REGISTRY NUMBER
COMMENTARY
9024-27-5
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(E,Z)-3-(3-indolyl)propanal oxime
?
Substrates: 51% activity compared to (E,Z)-indolyl-3-acetaldoxime
Products: -
Products: -
?
(E,Z)-4-(3-indolyl)butanal oxime
?
Substrates: 12% activity compared to (E,Z)-indolyl-3-acetaldoxime
Products: -
Products: -
?
(E,Z)-4-hydroxyphenylacetaldehyde oxime
?
Substrates: 30% activity compared to (E,Z)-indolyl-3-acetaldoxime
Products: -
Products: -
?
(E,Z)-4-methoxyphenylacetaldoxime
?
Substrates: 19% activity compared to (E,Z)-indolyl-3-acetaldoxime
Products: -
Products: -
?
(E,Z)-indolyl-3-acetaldoxime
(E,Z)-indolyl-3-acetonitrile
Substrates: 100% activity
Products: -
Products: -
r
3-Indoleacetaldoxime
3-Indoleacetonitrile
-
Substrates: -
Products: -
Products: -
?
3-Indoleacetaldoxime
3-Indoleacetonitrile
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme displays no activity toward (E,Z)-indole-3-carboxaldehyde oxime, (E,Z)-naphthyl-1-carboxaldehyde oxime, (E,Z)-naphthyl-2-carboxaldehyde oxime, (E,Z)-phenylacetaldoxime, (E,Z)-butanal oxime, (E,Z)-3-methylbutanal oxime, and (E,Z)-cyclopentanecarboxaldehyde oxime
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme displays no activity toward (E,Z)-indole-3-carboxaldehyde oxime, (E,Z)-naphthyl-1-carboxaldehyde oxime, (E,Z)-naphthyl-2-carboxaldehyde oxime, (E,Z)-phenylacetaldoxime, (E,Z)-butanal oxime, (E,Z)-3-methylbutanal oxime, and (E,Z)-cyclopentanecarboxaldehyde oxime
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Fe2+
addition of 1 mM FeCl2 results in a slight increase of enzyme activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
8-hydroxyquinoline
-
inhibition is partly reversed by ferric citrate, ascorbic acid and dehydroascorbic acid
NaBH4
-
inhibition is partly reversed by pyridoxal-5'-phosphate or dehydroascorbic acid
2,3-Dimercaptopropanol
-
reversal by dehydroascorbic acid, pyridoxal 5'-phosphate or frozen storage
additional information
no significant inhibition or activation of the enzyme occurs in the presence of dithiothreitol, FeCl3, NaN3, PLP, and FAD
-
additional information
-
no significant inhibition or activation of the enzyme occurs in the presence of dithiothreitol, FeCl3, NaN3, PLP, and FAD
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Na2S2O4
the specific activity of IADSs increases about 17fold upon addition of Na2S2O4 under anaerobic conditions
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
Arabidopsis cytochrome P450 monooxygenase 71A13 catalyzes the conversion of indole-3-acetaldoxime in camalexin synthesis.
Infections
The role of CYP71A12 monooxygenase in pathogen-triggered tryptophan metabolism and Arabidopsis immunity.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.29
(E,Z)-indolyl-3-acetaldoxime
in 25 mM Tris-HCl buffer pH 7.5, at 23°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
10
(E,Z)-indolyl-3-acetaldoxime
in 25 mM Tris-HCl buffer pH 7.5, at 23°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0045
crude extract, in 25 mM Tris-HCl buffer pH 7.5, at 23°C
0.175
after 39fold purification, in 25 mM Tris-HCl buffer pH 7.5, at 23°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9
-
pH 6.0: about 60% of maximal activity, pH 9.0: about 35% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
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). A7E8M5_SCLS1
Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1)
347
0
39023
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
homology modeling of structure. The heme resides between H-helix and J-helix in the hydrophobic pocket, where residues Gly305 and Thr308, 311 of the H-helix are involved in its stabilization. Substrate indole-3-acetaldoxime is tightly fitted into the substrate. The smaller size of the substrate binding pocket is due to the bulkiness of the two amino acid residues Phe182 and Trp315 pointing into the substrate binding cavity. The heme tethers the substrate during catalysis
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hydroxyapatite column chromatography, DEAE Sephacel gel filtration, and Superdex G-75 gel filtration
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kumar, S.A.; Mahadevan, S.
3-Indoleacetaldoxime hydro-lyase: a pyridoxal-5'-phosphate activated enzyme
Arch. Biochem. Biophys.
103
516-518
1963
Fusarium fujikuroi
brenda
Mahadevan, S.
Conversion of 3-indoleacetaldoxime to 3-indoleacetonitrile by plants
Arch. Biochem. Biophys.
100
557-558
1963
Fusarium fujikuroi, Aspergillus niger, Penicillium chrysogenum, Fusarium oxysporum, Musa acuminata
-
brenda
Shulka, P.S.; Mahadevan, S.
Indoleacetaldoxime hydro-lyase. II. Purification and properties
Arch. Biochem. Biophys.
125
873-883
1968
Fusarium fujikuroi
brenda
Shulka, P.S.; Mahadevan, S.
Indoleacetaldoxime hydro-lyase (4.2.1.29). III. Further studies on the nature and mode of action of the enzyme
Arch. Biochem. Biophys.
137
166-174
1970
Fusarium fujikuroi
brenda
Pedras, M.S.; Minic, Z.; Thongbam, P.D.; Bhaskar, V.; Montaut, S.
Indolyl-3-acetaldoxime dehydratase from the phytopathogenic fungus Sclerotinia sclerotiorum: purification, characterization, and substrate specificity
Phytochemistry
71
1952-1962
2010
Sclerotinia sclerotiorum (A7E8M5), Sclerotinia sclerotiorum
brenda
Kumari, V.; Kumar, V.; Bhalla, T.C.
Functional interpretation and structural insights of Arabidopsis lyrata cytochrome P450 CYP71A13 involved in auxin synthesis
Bioinformation
11
330-335
2015
Arabidopsis lyrata subsp. lyrata (D7LC87)
brenda
EXTERNAL LINKS (specific for EC-Number 4.8.1.3)
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