Information on EC 1.1.3.42 - prosolanapyrone-II oxidase

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The expected taxonomic range for this enzyme is: Alternaria solani

EC NUMBER
COMMENTARY hide
1.1.3.42
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RECOMMENDED NAME
GeneOntology No.
prosolanapyrone-II oxidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
prosolanapyrone II + O2 = prosolanapyrone III + H2O2
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
prosolanapyrone-II:oxygen 3'-oxidoreductase
The enzyme is involved in the biosynthesis of the phytotoxin solanapyrone by some fungi. The bifunctional enzyme catalyses the oxidation of prosolanapyrone II and the subsequent Diels Alder cycloisomerization of the product prosolanapyrone III to (-)-solanapyrone A (cf. EC 5.5.1.20, prosolanapyrone III cycloisomerase).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
prosolanapyrone II + O2
prosolanapyrone III + H2O2
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
prosolanapyrone II + O2
prosolanapyrone III + H2O2
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
flavin
additional information
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the activity of solanapyrone synthase is not affected by NAD+, NADP+, FMN, and FAD+
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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the activity of solanapyrone synthase is not affected by divalent cations
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.016
prosolanapyrone II
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in 50 mM potassium phosphate buffer, pH 7.0, at 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00084
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crude extract, in 50 mM potassium phosphate buffer, pH 7.0, at 30°C
0.00104
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crude extract, pH 7.0, 30°C
0.0206
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after 25fold purification, in 50 mM potassium phosphate buffer, pH 7.0, at 30°C
1.69
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after 1630 fold purification, pH 7.0, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
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in sodium acetate buffer
7.5
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in Tris buffer
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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assay at
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
46000 - 62000
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native enzyme, gel filtration
53000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 41000, truncated solanapyrone synthase, SDS-PAGE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.7
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irreversible inactivation is observed below pH 3.7
714292
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
solanapyrone synthase activity is rather unstable in both crude and partially purified states. It loses 55% of its activity after 36 h at 4°C but the addition of 30% glycerol markedly improves stability, the preparation retains 55% activity for 9 days at 4°C. Other additives such as EDTA, thiol reagents and reducing agents are not effective
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-84°C, purified enzyme in 50 mM potassium phosphate buffer pH 7.0 in the presence of 30% (v/v) glycerol, 5 months, 14% loss of activity
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4°C, crude and partially purified states in the presence of 30% glycerol, 9 days, 45% loss of activity
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4°C, crude and partially purified states, 36 h, 55% loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, DEAE-Sepharose column chromatography, preparative isoelectric focusing, and phenyl-Sepharose column chromatography
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partial purification by ammonium sulfate precipitation and DEAE-Sepharose column chromatography
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phenyl Sepharose column chromatography, Mono Q column chromatography, DEAE-cellulose column chromatography, and Superdex 200 gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Aspergillus oryzae under the starch inducible alpha-amylase promoter, expression in Pichia pastoris
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