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Information on EC 1.1.3.42 - prosolanapyrone-II oxidase
for references in articles please use BRENDA:EC1.1.3.42
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.3 With oxygen as acceptor
1.1.3.42 prosolanapyrone-II oxidase
IUBMB Comments
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).
The enzyme appears in viruses and cellular organisms
- 1.1.3.42
- solani
-
alternaria
-
diels-alder
-
diels-alderase
-
iterative
-
cycloaddition
- polyketide
showSynonyms
solanapyrone synthase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Sol5
solanapyrone synthase
SPS
solanapyrone synthase
bifunctional enzyme: prosolanapyrone II oxidase/prosolanapyrone III cycloisomerase
solanapyrone synthase
bifunctional enzyme: prosolanapyrone II oxidase/prosolanapyrone III cycloisomerase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
prosolanapyrone II + O2 = prosolanapyrone III + H2O2
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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).
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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
prosolanapyrone II + O2
prosolanapyrone III + H2O2
-
Substrates: -
Products: -
Products: -
r
prosolanapyrone II + O2
prosolanapyrone III + H2O2
Substrates: -
Products: -
Products: -
?
prosolanapyrone II + O2
prosolanapyrone III + H2O2
Substrates: the enzyme is involved in solanapyrone biosynthesis
Products: -
Products: -
?
prosolanapyrone II + O2
prosolanapyrone III + H2O2
Substrates: the bifunctional enzyme catalyses the oxidation of prosolanapyrone II and the subsequent cycloaddition of the product prosolanapyrone III to (-)-solanapyrone A
Products: in an enzyme-catalyzed DielsAlder reaction the product prosolanapyrone III is isomerized to solanapyrone A (exo Diels-Alder cyclization, [4+2] cycloaddition). Solanapyrone D (endo Diels-Alder cyclization) is formed by a nonenzymatic Diels-Alder cyclization of prosolanopyrone III in polar solvents. The enzyme coverts prosolanapyrone II into solanapyrone A, solanapyrone D and prosolanapyrone III in the ratio 7:1:1
Products: in an enzyme-catalyzed DielsAlder reaction the product prosolanapyrone III is isomerized to solanapyrone A (exo Diels-Alder cyclization, [4+2] cycloaddition). Solanapyrone D (endo Diels-Alder cyclization) is formed by a nonenzymatic Diels-Alder cyclization of prosolanopyrone III in polar solvents. The enzyme coverts prosolanapyrone II into solanapyrone A, solanapyrone D and prosolanapyrone III in the ratio 7:1:1
?
prosolanapyrone II + O2
prosolanapyrone III + H2O2
Substrates: the enzyme is involved in solanapyrone biosynthesis
Products: -
Products: -
?
prosolanapyrone II + O2
prosolanapyrone III + H2O2
Substrates: the bifunctional enzyme catalyses the oxidation of prosolanapyrone II and the subsequent cycloaddition of the product prosolanapyrone III to (-)-solanapyrone A
Products: in an enzyme-catalyzed DielsAlder reaction the product prosolanapyrone III is isomerized to solanapyrone A (exo Diels-Alder cyclization, [4+2] cycloaddition). Solanapyrone D (endo Diels-Alder cyclization) is formed by a nonenzymatic Diels-Alder cyclization of prosolanopyrone III in polar solvents. The enzyme coverts prosolanapyrone II into solanapyrone A, solanapyrone D and prosolanapyrone III in the ratio 7:1:1
Products: in an enzyme-catalyzed DielsAlder reaction the product prosolanapyrone III is isomerized to solanapyrone A (exo Diels-Alder cyclization, [4+2] cycloaddition). Solanapyrone D (endo Diels-Alder cyclization) is formed by a nonenzymatic Diels-Alder cyclization of prosolanopyrone III in polar solvents. The enzyme coverts prosolanapyrone II into solanapyrone A, solanapyrone D and prosolanapyrone III in the ratio 7:1:1
?
prosolanapyrone II + O2
prosolanapyrone III + H2O2
Substrates: -
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
prosolanapyrone II + O2
prosolanapyrone III + H2O2
Substrates: -
Products: -
Products: -
?
prosolanapyrone II + O2
prosolanapyrone III + H2O2
Substrates: the enzyme is involved in solanapyrone biosynthesis
Products: -
Products: -
?
prosolanapyrone II + O2
prosolanapyrone III + H2O2
Substrates: the enzyme is involved in solanapyrone biosynthesis
Products: -
Products: -
?
prosolanapyrone II + O2
prosolanapyrone III + H2O2
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the activity of solanapyrone synthase is not affected by NAD+, NADP+, FMN, and FAD+
-
flavin
flavin-dependent oxidase, the enzyme possesses a flavin-binding domain
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the activity of solanapyrone synthase is not affected by divalent cations
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.016
prosolanapyrone II
-
in 50 mM potassium phosphate buffer, pH 7.0, at 30°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00084
-
crude extract, in 50 mM potassium phosphate buffer, pH 7.0, at 30°C
0.0206
-
after 25fold purification, in 50 mM potassium phosphate buffer, pH 7.0, at 30°C
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pH OPTIMUM
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
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). SOL5_ALTSO
515
0
55994
Swiss-Prot
Secretory Pathway (Reliability: 2)
A0A5K1JXB5_9APHY
715
0
77831
TrEMBL
other Location (Reliability: 1)
A0A5K1K6H9_9APHY
569
0
63425
TrEMBL
other Location (Reliability: 2)
A0A5K1JU65_9APHY
315
0
35233
TrEMBL
Secretory Pathway (Reliability: 5)
A0A5K1JUD7_9APHY
142
0
15843
TrEMBL
Mitochondrion (Reliability: 5)
A0A8J8W7R3_9EURO
502
0
53546
TrEMBL
Secretory Pathway (Reliability: 2)
A0A084FUZ4_PSEDA
616
0
68392
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5K1JXY4_9APHY
494
0
55864
TrEMBL
other Location (Reliability: 1)
A0A5K1K8T5_9APHY
119
0
12665
TrEMBL
Mitochondrion (Reliability: 3)
A0A5K1JZI1_9APHY
84
0
9154
TrEMBL
other Location (Reliability: 4)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
-
4°C, crude and partially purified states in the presence of 30% glycerol, 9 days, 45% 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
-
partial purification by ammonium sulfate precipitation and DEAE-Sepharose column chromatography
-
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Katayama, K.; Kobayashi, T.; Oikawa, H.; Honma, M.; Ichihara, A.
Enzymatic activity and partial purification of solanapyrone synthase: First enzyme catalyzing Diels-Alder reaction
Biochim. Biophys. Acta
1384
387-395
1998
Alternaria solani
brenda
Katayama, K.; Kobayashi, T.; Chijimatsu, M.; Ichihara, A.; Oikawa, H.
Purification and N-terminal amino acid sequence of solanapyrone synthase, a natural Diels-Alderase from Alternaria solani
Biosci. Biotechnol. Biochem.
72
604-607
2008
Alternaria solani
brenda
Kasahara, K.; Miyamoto, T.; Fujimoto, T.; Oguri, H.; Tokiwano, T.; Oikawa, H.; Ebizuka, Y.; Fujii, I.
Solanapyrone synthase, a possible Diels-Alderase and iterative type I polyketide synthase encoded in a biosynthetic gene cluster from Alternaria solani
ChemBioChem
11
1245-1252
2010
Alternaria solani (D7UQ40), Alternaria solani, Alternaria solani 548 (D7UQ40)
brenda
Fujii, I.
Functional analysis of fungal polyketide biosynthesis genes
J. Antibiot.
63
207-218
2010
Alternaria solani (D7UQ40), Alternaria solani, Alternaria solani 548 (D7UQ40)
brenda
Kim, W.; Park, C.M.; Park, J.J.; Akamatsu, H.O.; Peever, T.L.; Xian, M.; Gang, D.R.; Vandemark, G.; Chen, W.
Functional analyses of the Diels-alderase gene sol5 of Ascochyta rabiei and Alternaria solani indicate that the solanapyrone phytotoxins are not required for pathogenicity
Mol. Plant Microbe Interact.
28
482-496
2015
Ascochyta rabiei (A0A097PUG9), Alternaria solani (D7UQ40)
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.3.42)
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Release 2023.1 (January 2023)
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