Enzymes
| UniProtKB help_outline | 8 proteins |
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- Name help_outline (2E,6E)-farnesyl diphosphate Identifier CHEBI:175763 Charge -3 Formula C15H25O7P2 InChIKeyhelp_outline VWFJDQUYCIWHTN-YFVJMOTDSA-K SMILEShelp_outline CC(C)=CCC\C(C)=C\CC\C(C)=C\COP([O-])(=O)OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 175 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 3,5-dimethylorsellinate Identifier CHEBI:131856 Charge -1 Formula C10H11O4 InChIKeyhelp_outline NZGSNQJCTOMELT-UHFFFAOYSA-M SMILEShelp_outline C=1(C(=C(C(=C(C1C)O)C(=O)[O-])C)C)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 (3R)-3-farnesyl-6-hydroxy-2,3,5-trimethyl-4-oxocyclohexa-1,5-diene-1-carboxylate Identifier CHEBI:131857 Charge -2 Formula C25H34O4 InChIKeyhelp_outline BAJLPQKQXYOBIY-MNPZXIHOSA-L SMILEShelp_outline C1([C@@](C(=C(C(=C1C)[O-])C(=O)[O-])C)(C/C=C(/CC/C=C(/CCC=C(C)C)\C)\C)C)=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 diphosphate Identifier CHEBI:33019 (Beilstein: 185088) help_outline Charge -3 Formula HO7P2 InChIKeyhelp_outline XPPKVPWEQAFLFU-UHFFFAOYSA-K SMILEShelp_outline OP([O-])(=O)OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 1,129 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
Cross-references
| RHEA:49632 | RHEA:49633 | RHEA:49634 | RHEA:49635 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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Novofumigatonin biosynthesis involves a non-heme iron-dependent endoperoxide isomerase for orthoester formation.
Matsuda Y., Bai T., Phippen C.B.W., Noedvig C.S., Kjaerboelling I., Vesth T.C., Andersen M.R., Mortensen U.H., Gotfredsen C.H., Abe I., Larsen T.O.
Novofumigatonin (1), isolated from the fungus Aspergillus novofumigatus, is a heavily oxygenated meroterpenoid containing a unique orthoester moiety. Despite the wide distribution of orthoesters in nature and their biological importance, little is known about the biogenesis of orthoesters. Here we ... >> More
Novofumigatonin (1), isolated from the fungus Aspergillus novofumigatus, is a heavily oxygenated meroterpenoid containing a unique orthoester moiety. Despite the wide distribution of orthoesters in nature and their biological importance, little is known about the biogenesis of orthoesters. Here we show the elucidation of the biosynthetic pathway of 1 and the identification of key enzymes for the orthoester formation by a series of CRISPR-Cas9-based gene-deletion experiments and in vivo and in vitro reconstitutions of the biosynthesis. The novofumigatonin pathway involves endoperoxy compounds as key precursors for the orthoester synthesis, in which the Fe(II)/α-ketoglutarate-dependent enzyme NvfI performs the endoperoxidation. NvfE, the enzyme catalyzing the orthoester synthesis, is an Fe(II)-dependent, but cosubstrate-free, endoperoxide isomerase, despite the fact that NvfE shares sequence homology with the known Fe(II)/α-ketoglutarate-dependent dioxygenases. NvfE thus belongs to a class of enzymes that gained an isomerase activity by losing the α-ketoglutarate-binding ability. << Less
Nat. Commun. 9:2587-2587(2018) [PubMed] [EuropePMC]
This publication is cited by 13 other entries.
Comments
Published in: Itoh, T., Tokunaga, K., Radhakrishnan, E.K., Fujii, I., Abe, I. Ebizuka, Y. and Kushiro, T. Identification of a key prenyltransferase involved in biosynthesis of the most abundant fungal meroterpenoids derived from 3,5-dimethylorsellinic acid.