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- Name help_outline prosolanapyrone III Identifier CHEBI:63164 Charge 0 Formula C18H22O4 InChIKeyhelp_outline KINNIEOBQSTCFI-JHHIBIJLSA-N SMILEShelp_outline [H]C(=O)c1c(OC)cc(\C=C\CCCC\C=C\C=C\C)oc1=O 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (-)-solanapyrone A Identifier CHEBI:38229 (Beilstein: 4711945; CAS: 88899-61-0) help_outline Charge 0 Formula C18H22O4 InChIKeyhelp_outline AWQLNKJBXASXDU-SFDCBXKLSA-N SMILEShelp_outline [H]C(=O)c1c(OC)cc(oc1=O)[C@@H]1[C@@H](C)C=C[C@@]2([H])CCCC[C@@]12[H] 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:31683 | RHEA:31684 | RHEA:31685 | RHEA:31686 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Purification and N-terminal amino acid sequence of solanapyrone synthase, a natural Diels-Alderase from Alternaria solani.
Katayama K., Kobayashi T., Chijimatsu M., Ichihara A., Oikawa H.
The first natural Diels-Alderase, solanapyrone synthase, was purified 1,630-fold from a crude extract. The 41-kDa protein on SDS-polyacrylamide gel electrophoresis was identified as truncated solanapyrone synthase, and its N-terminal amino acid sequence was found to be QETQNLNNFLESNAINP.
Biosci. Biotechnol. Biochem. 72:604-607(2008) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Solanapyrone synthase, a possible Diels-Alderase and iterative type I polyketide synthase encoded in a biosynthetic gene cluster from Alternaria solani.
Kasahara K., Miyamoto T., Fujimoto T., Oguri H., Tokiwano T., Oikawa H., Ebizuka Y., Fujii I.
The solanapyrone biosynthetic gene cluster was cloned from Alternaria solani. It consists of six genes-sol1-6-coding for a polyketide synthase, an O-methyltransferase, a dehydrogenase, a transcription factor, a flavin-dependent oxidase, and cytochrome P450. The prosolanapyrone synthase (PSS) encod ... >> More
The solanapyrone biosynthetic gene cluster was cloned from Alternaria solani. It consists of six genes-sol1-6-coding for a polyketide synthase, an O-methyltransferase, a dehydrogenase, a transcription factor, a flavin-dependent oxidase, and cytochrome P450. The prosolanapyrone synthase (PSS) encoded by sol1 was expressed in Aspergillus oryzae and its product was identified as desmethylprosolanapyrone I (8). Although PSS is closely related to the PKSs/Diels-Alderases LovB and MlcA of lovastatin and compactin biosynthesis, it did not catalyze cycloaddition. Sol5, encoding a flavin-dependent oxidase (solanapyrone synthase, SPS), was expressed in Pichia pastoris and purified. The purified recombinant SPS showed activity for the formation of (-)-solanapyrone A (1) from achiral prosolanapyrone II (2), establishing that this single enzyme catalyzes both the oxidation and the subsequent cycloaddition reaction, possibly as a Diels-Alder enzyme. << Less
ChemBioChem 11:1245-1252(2010) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Enzymatic activity and partial purification of solanapyrone synthase: first enzyme catalyzing Diels-Alder reaction.
Katayama K., Kobayashi T., Oikawa H., Honma M., Ichihara A.
In cell-free extracts of Alternaria solani, an enzymatic activity converting prosolanapyrone II to solanapyrones A and D via oxidation and subsequent Diels-Alder reaction has been found. Chromatography with DEAE-Sepharose provided two active fractions, pools 1 and 2. The former fraction converted ... >> More
In cell-free extracts of Alternaria solani, an enzymatic activity converting prosolanapyrone II to solanapyrones A and D via oxidation and subsequent Diels-Alder reaction has been found. Chromatography with DEAE-Sepharose provided two active fractions, pools 1 and 2. The former fraction converted prosolanapyrone II to solanapyrones A and D in a ratio of 2.2:1 with optical purities of 99% and 45% ee, respectively. The latter fraction did so in a ratio of 7.6:1 with 99% and nearly 0% ee, respectively. The enzyme partially purified from pool 2 native molecular weight of 40-62 kD and a pl of 4.25. The high reactivity of prosolanapyrone III in aqueous solution and the chromatographic behavior of the enzyme in pool 2 suggest that a single enzyme catalyzes both the oxidation and Diels-Alder reaction. << Less
Biochim. Biophys. Acta 1384:387-395(1998) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.