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
LITERATURE
(indol-3-yl)acetaldehyde oxime = (indol-3-yl)acetonitrile + H2O
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
camalexin biosynthesis
-
-
indole-3-acetate biosynthesis II
-
-
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
COMMENTARY
LITERATURE
dehydratase, indoleacetaldoxime
-
-
-
-
EC 4.2.1.29
-
-
formerly
-
indoleacetaldoxime hydro-lyase
-
-
-
-
indolyl-3-acetaldoxime dehydratase
-
protein SS1G-01653
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CAS REGISTRY NUMBER
COMMENTARY
9024-27-5
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
var. cubense
-
-
Manually annotated by BRENDA team
banana
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
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
51% activity compared to (E,Z)-indolyl-3-acetaldoxime
-
-
?
(E,Z)-4-(3-indolyl)butanal oxime
?
show the reaction diagram
12% activity compared to (E,Z)-indolyl-3-acetaldoxime
-
-
?
(E,Z)-4-hydroxyphenylacetaldehyde oxime
?
show the reaction diagram
30% activity compared to (E,Z)-indolyl-3-acetaldoxime
-
-
?
(E,Z)-4-methoxyphenylacetaldoxime
?
show the reaction diagram
19% activity compared to (E,Z)-indolyl-3-acetaldoxime
-
-
?
(E,Z)-indolyl-3-acetaldoxime
(E,Z)-indolyl-3-acetonitrile
show the reaction diagram
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
-
-
-
-
3-Indoleacetaldoxime
3-Indoleacetonitrile
show the reaction diagram
-
-
-
-
additional information
?
-
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
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
cofactor
pyridoxal 5'-phosphate
-
required
pyridoxal 5'-phosphate
-
activates
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
-
activates, no activation by Fe3+
Fe2+
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
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
Benzaldoxime
-
-
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
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
dehydroascorbic acid
-
activates
dihydrofolic acid
-
activates
glutathione
-
activates
Na2S2O4
the specific activity of IADSs increases about 17fold upon addition of Na2S2O4 under anaerobic conditions
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 23C
0.17
3-indoleacetaldoxime
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
10
(E,Z)-indolyl-3-acetaldoxime
Sclerotinia sclerotiorum
A7E8M5
in 25 mM Tris-HCl buffer pH 7.5, at 23C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0045
crude extract, in 25 mM Tris-HCl buffer pH 7.5, at 23C
0.175
after 39fold purification, in 25 mM Tris-HCl buffer pH 7.5, at 23C
additional information
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-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9
-
pH 6.0: about 60% of maximal activity, pH 9.0: about 35% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
41000
calculated from amino acid sequence
716456
44000
gel filtration
716456
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
1 * 44000, SDS-PAGE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 7
-
maximally stable
648796
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hydroxyapatite column chromatography, DEAE Sephacel gel filtration, and Superdex G-75 gel filtration