Information on EC 4.99.1.6 - indoleacetaldoxime dehydratase

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY
4.99.1.6
-
RECOMMENDED NAME
GeneOntology No.
indoleacetaldoxime dehydratase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
(indol-3-yl)acetaldehyde oxime = (indol-3-yl)acetonitrile + H2O
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
elimination
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
camalexin biosynthesis
-
indole-3-acetate biosynthesis II
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Tryptophan metabolism
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SYSTEMATIC NAME
IUBMB Comments
(indol-3-yl)acetaldehyde-oxime hydro-lyase [(indol-3-yl)acetonitrile-forming]
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SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dehydratase, indoleacetaldoxime
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-
-
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EC 4.2.1.29
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-
formerly
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indoleacetaldoxime hydro-lyase
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-
-
-
indolyl-3-acetaldoxime dehydratase
A7E8M5
-
protein SS1G-01653
A7E8M5
-
CAS REGISTRY NUMBER
COMMENTARY
9024-27-5
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
var. cubense
-
-
Manually annotated by BRENDA team
banana
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-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(E,Z)-3-(3-indolyl)propanal oxime
?
show the reaction diagram
A7E8M5, -
51% activity compared to (E,Z)-indolyl-3-acetaldoxime
-
-
?
(E,Z)-4-(3-indolyl)butanal oxime
?
show the reaction diagram
A7E8M5, -
12% activity compared to (E,Z)-indolyl-3-acetaldoxime
-
-
?
(E,Z)-4-hydroxyphenylacetaldehyde oxime
?
show the reaction diagram
A7E8M5, -
30% activity compared to (E,Z)-indolyl-3-acetaldoxime
-
-
?
(E,Z)-4-methoxyphenylacetaldoxime
?
show the reaction diagram
A7E8M5, -
19% activity compared to (E,Z)-indolyl-3-acetaldoxime
-
-
?
(E,Z)-indolyl-3-acetaldoxime
(E,Z)-indolyl-3-acetonitrile
show the reaction diagram
A7E8M5, -
100% activity
-
-
r
3-Indoleacetaldoxime
3-Indoleacetonitrile
show the reaction diagram
-
-
-
-
3-Indoleacetaldoxime
3-Indoleacetonitrile
show the reaction diagram
-
-
-
-
3-Indoleacetaldoxime
3-Indoleacetonitrile
show the reaction diagram
-
-
-
-
3-Indoleacetaldoxime
3-Indoleacetonitrile
show the reaction diagram
-
-
-
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3-Indoleacetaldoxime
3-Indoleacetonitrile
show the reaction diagram
-
-
-
-
additional information
?
-
A7E8M5, -
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
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-
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COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
cofactor
pyridoxal 5'-phosphate
-
required
pyridoxal 5'-phosphate
-
activates
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Fe2+
-
activates, no activation by Fe3+
Fe2+
A7E8M5, -
addition of 1 mM FeCl2 results in a slight increase of enzyme activity
Fe3+
-
Ferric citrate promotes activity
KCN
-
activates at 0.001-0.1 mM, inhibits at 1-10 mM
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2,3-Dimercaptopropanol
-
-
2,3-Dimercaptopropanol
-
reversal by dehydroascorbic acid, pyridoxal 5'-phosphate or frozen storage
2-mercaptoethanol
-
-
8-hydroxyquinoline
-
inhibition is partly reversed by ferric citrate, ascorbic acid and dehydroascorbic acid
Ag+
-
1 mM, complete inactivation
Al3+
-
1 mM, complete inactivation
Cu2+
-
1 mM, complete inactivation
Diethyl dithiocarbamate
-
-
Hg2+
-
1 mM, complete inactivation
KCN
-
activates at 0.001-0.1 mM, inhibits at 1-10 mM
KCN
-
reversed by pyridoxal 5'-phosphate
Mandelaldoxime
-
-
Mercaptoacetic acid
-
weak
NaBH4
-
inhibition is partly reversed by pyridoxal-5'-phosphate or dehydroascorbic acid
NEM
-
protection by phenylacetaldoxime
p-hydroxymercuribenzoate
-
-
phenylacetaldoxime
-
competitive
Phenylpropionaldoxime
-
-
Phenylthiocyanate
-
-
tetrahydrofolic acid
-
-
Zn2+
-
1 mM, complete inactivation
Mo5+
-
1 mM, complete inactivation
additional information
A7E8M5, -
no significant inhibition or activation of the enzyme occurs in the presence of dithiothreitol, FeCl3, NaN3, PLP, and FAD
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
dehydroascorbic acid
-
activates
dihydrofolic acid
-
activates
glutathione
-
activates
Na2S2O4
A7E8M5, -
the specific activity of IADSs increases about 17fold upon addition of Na2S2O4 under anaerobic conditions
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.29
-
(E,Z)-indolyl-3-acetaldoxime
A7E8M5, -
in 25 mM Tris-HCl buffer pH 7.5, at 23C
-
0.17
-
3-Indoleacetaldoxime
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-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
10
-
(E,Z)-indolyl-3-acetaldoxime
A7E8M5, -
in 25 mM Tris-HCl buffer pH 7.5, at 23C
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0045
-
A7E8M5, -
crude extract, in 25 mM Tris-HCl buffer pH 7.5, at 23C
0.175
-
A7E8M5, -
after 39fold purification, in 25 mM Tris-HCl buffer pH 7.5, at 23C
additional information
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-
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pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.2
7.5
A7E8M5, -
at 25C
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
9
-
pH 6.0: about 60% of maximal activity, pH 9.0: about 35% of maximal activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
-
A7E8M5, -
calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
41000
-
A7E8M5, -
calculated from amino acid sequence
44000
-
A7E8M5, -
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
monomer
A7E8M5, -
1 * 44000, SDS-PAGE
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
7
-
maximally stable
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hydroxyapatite column chromatography, DEAE Sephacel gel filtration, and Superdex G-75 gel filtration
A7E8M5, -