Enzymes
UniProtKB help_outline | 2 proteins |
Reaction participants Show >> << Hide
- Name help_outline AH2 Identifier CHEBI:17499 Charge 0 Formula RH2 SMILEShelp_outline *([H])[H] 2D coordinates Mol file for the small molecule Search links Involved in 2,799 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline dehydroprobetaenone I Identifier CHEBI:145061 Charge 0 Formula C21H34O2 InChIKeyhelp_outline BINVZINZKJFBTL-QQJLSPJJSA-N SMILEShelp_outline [C@]1([C@H](C(=C[C@@]2([C@@]1([C@@H](C[C@@H](C2)C)C)[H])[H])C)[C@@H](CC)C)(C(=O)/C=C\O)C 2D coordinates Mol file for the small molecule Search links Involved in 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline A Identifier CHEBI:13193 Charge Formula R SMILEShelp_outline * 2D coordinates Mol file for the small molecule Search links Involved in 2,870 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline probetaenone I Identifier CHEBI:145062 Charge 0 Formula C21H36O2 InChIKeyhelp_outline CWVNYXDUEQFYMM-YDGZXZOGSA-N SMILEShelp_outline [C@]1([C@H](C(=C[C@@]2([C@@]1([C@@H](C[C@@H](C2)C)C)[H])[H])C)[C@@H](CC)C)(C(=O)CCO)C 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:61864 | RHEA:61865 | RHEA:61866 | RHEA:61867 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
UniProtKB help_outline |
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Publications
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Biosynthesis of a Tricyclo[6.2.2.02,7]dodecane System by a Berberine Bridge Enzyme-like Intramolecular Aldolase.
Li H., Hu J., Wei H., Solomon P.S., Stubbs K.A., Chooi Y.H.
The aldol reaction is one of the most fundamental stereocontrolled carbon-carbon bond-forming reactions and is mainly catalyzed by aldolases in nature. Despite the fact that the aldol reaction has been widely proposed to be involved in fungal secondary metabolite biosynthesis, a dedicated aldolase ... >> More
The aldol reaction is one of the most fundamental stereocontrolled carbon-carbon bond-forming reactions and is mainly catalyzed by aldolases in nature. Despite the fact that the aldol reaction has been widely proposed to be involved in fungal secondary metabolite biosynthesis, a dedicated aldolase that catalyzes stereoselective aldol reactions has only rarely been reported in fungi. Herein, we activated a cryptic polyketide biosynthetic gene cluster that was upregulated in the fungal wheat pathogen Parastagonospora nodorum during plant infection; this resulted in the production of the phytotoxic stemphyloxin II (1). Through heterologous reconstruction of the biosynthetic pathway and in vitro assay by using cell-free lysate from Aspergillus nidulans, we demonstrated that a berberine bridge enzyme (BBE)-like protein SthB catalyzes an intramolecular aldol reaction to establish the bridged tricyclo[6.2.2.0<sup>2,7</sup> ]dodecane skeleton in the post-assembly tailoring step. The characterization of SthB as an aldolase enriches the catalytic toolbox of classic reactions and the functional diversities of the BBE superfamily of enzymes. << Less
Chemistry 25:15062-15066(2019) [PubMed] [EuropePMC]
This publication is cited by 9 other entries.
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Heterologous expression of highly reducing polyketide synthase involved in betaenone biosynthesis.
Ugai T., Minami A., Fujii R., Tanaka M., Oguri H., Gomi K., Oikawa H.
A unique highly reducing polyketide synthase (HR-PKS) with a reductase domain was identified in a betaenone biosynthetic gene cluster. Successful heterologous expression and characterization of the HR-PKS and trans-acting enoyl reductase (ER) provide insights into the core structure formation with ... >> More
A unique highly reducing polyketide synthase (HR-PKS) with a reductase domain was identified in a betaenone biosynthetic gene cluster. Successful heterologous expression and characterization of the HR-PKS and trans-acting enoyl reductase (ER) provide insights into the core structure formation with a decalin scaffold and allow reconstitution of the betaenone biosynthetic machinery. << Less
Chem. Commun. (Camb.) 51:1878-1881(2015) [PubMed] [EuropePMC]
This publication is cited by 5 other entries.