Enzymes
| UniProtKB help_outline | 2 proteins |
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- Name help_outline fonsecin B Identifier CHEBI:133825 (CAS: 1856-95-7) help_outline Charge 0 Formula C16H16O6 InChIKeyhelp_outline ZYTKFYQKQVYVMW-UHFFFAOYSA-N SMILEShelp_outline C12=C(C=3C(=CC(=CC3C=C1OC(CC2=O)(O)C)OC)OC)O 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
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,431 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline NADPH Identifier CHEBI:57783 (Beilstein: 10411862) help_outline Charge -4 Formula C21H26N7O17P3 InChIKeyhelp_outline ACFIXJIJDZMPPO-NNYOXOHSSA-J SMILEShelp_outline NC(=O)C1=CN(C=CC1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](OP([O-])([O-])=O)[C@@H]2O)n2cnc3c(N)ncnc23)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,279 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline O2 Identifier CHEBI:15379 (CAS: 7782-44-7) help_outline Charge 0 Formula O2 InChIKeyhelp_outline MYMOFIZGZYHOMD-UHFFFAOYSA-N SMILEShelp_outline O=O 2D coordinates Mol file for the small molecule Search links Involved in 2,709 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline aurasperone B Identifier CHEBI:133756 (CAS: 41689-67-2) help_outline Charge 0 Formula C32H30O12 InChIKeyhelp_outline VIFQAHKDYKZMMS-UHFFFAOYSA-N SMILEShelp_outline C=1(C2=C(C=C(C1)OC)C(=C3C(=C2O)C(CC(O3)(C)O)=O)C=4C(=C5C(=CC4OC)C=C6C(=C5O)C(CC(O6)(C)O)=O)OC)OC 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
- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,204 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline NADP+ Identifier CHEBI:58349 Charge -3 Formula C21H25N7O17P3 InChIKeyhelp_outline XJLXINKUBYWONI-NNYOXOHSSA-K SMILEShelp_outline NC(=O)c1ccc[n+](c1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](OP([O-])([O-])=O)[C@@H]2O)n2cnc3c(N)ncnc23)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,285 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:62788 | RHEA:62789 | RHEA:62790 | RHEA:62791 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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Biaryl-forming enzymes from Aspergilli exhibit substrate-dependent stereoselectivity.
Obermaier S., Mueller M.
Natural biaryls typically occur as one regio- and atropisomeric variant in a given organism. Here, we report on the identification of biosynthetic genes of aurasperone- and bifonsecin-type biaryls in several Aspergillus species. The genes of the tailoring enzymes form a gene cluster that is separa ... >> More
Natural biaryls typically occur as one regio- and atropisomeric variant in a given organism. Here, we report on the identification of biosynthetic genes of aurasperone- and bifonsecin-type biaryls in several Aspergillus species. The genes of the tailoring enzymes form a gene cluster that is separate from the polyketide synthase gene. Dimerization of naphthopyrone monomers is catalyzed by members of an undescribed subfamily of cytochrome P450 enzymes. The stereoselectivity of these enzymes is influenced by the two natural monomeric substrates; homodimerization of one monomer yields a stereochemically pure biaryl, while the other monomer yields a mixture of enantiomers. << Less
Biochemistry 58:2589-2593(2019) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.