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FAD-binding monooxygenase

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FAD-binding monooxygenase; part of the gene cluster that mediates the biosynthesis of anditomin, a fungal meroterpenoid .

Below are the list of possible FAD-binding monooxygenase products. If you cannot find the target and/or product is not available in our catalog, please click here to contact us and request the product or submit your request for custom elisa kit production, custom recombinant protein production or custom antibody production. Custom ELISA Kits, Recombinant Proteins and Antibodies can be designed, manufactured and produced according to the researcher's specifications.
 

FAD-binding monooxygenase andJ

 FAD-binding monooxygenase andJ ELISA Kit
 FAD-binding monooxygenase andJ Recombinant
 FAD-binding monooxygenase andJ Antibody
Also known as FAD-binding monooxygenase andJ (Anditomin synthesis protein J).
FAD-binding monooxygenase; part of the gene cluster that mediates the biosynthesis of anditomin, a fungal meroterpenoid (PubMed:25216349). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase andM (PubMed:25216349). DMOA is then converted to the phthalide comp
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ound 5,7-dihydroxy-4,6-dimethylphthalide (DHDMP) by the cytochrome P450 monooxygenase andK, which is further prenylated by the prenyltransferase andD to yield farnesyl-DHDMP (PubMed:25216349). Further epoxidation by the FAD-dependent monooxygenase andE leads to epoxyfarnesyl-DHDMP (PubMed:25216349). The next step involves the terpene cyclase andB that converts epoxyfarnesyl-DHDMP into preandiloid A through opening of the epoxide ring followed by the cyclization of the farnesyl moiety (PubMed:25216349). Preandiloid A is in turn oxidized at the C-3 hydroxyl group to yield preandiloid B by the dehydrogenase andC (PubMed:25216349). The dioxygenase andA is solely responsible for the dehydrogenation of preandiloid B leading to the enone preandiloid C, as well as for the intriguing structural rearrangement to generate the bicyclo[2.2.2]octane core, transforming preandiloid C into andiconin (PubMed:25216349). FAD-binding monooxygenase andJ then produces andilesin D which is reduced by dehydrogenase andI to yield andilesin A (PubMed:25216349). Action of acetyltransferase andG followed by a spontaneous acetate elimination leads then to andilesin B, which is in turn substrate of the short chain dehydrogenase andH to yield andilesin C (PubMed:25216349). Finally, the dioxygenase andF catalyzes the transformation of andilesin C to anditomin (PubMed:25216349).
 andJ ELISA Kit
 andJ Recombinant
 andJ Antibody
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FAD-binding monooxygenase ausB

 FAD-binding monooxygenase ausB ELISA Kit
 FAD-binding monooxygenase ausB Recombinant
 FAD-binding monooxygenase ausB Antibody
Also known as FAD-binding monooxygenase ausB (Austinol synthesis protein B).
FAD-binding monooxygenase; part of the gene cluster A that mediates the biosynthesis of austinol and dehydroaustinol, two fungal meroterpenoids (PubMed:22329759). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (PubMed:22329759). 3,5-dimethylorsellinic acid
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is then prenylated by the polyprenyl transferase ausN (PubMed:22329759). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A (PubMed:22329759). Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE (PubMed:22329759, PubMed:23865690). Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4 (PubMed:22329759). The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide (PubMed:22329759). Finally, the cytochrome P450 monooxygenase ausG modifies austinolide to austinol (PubMed:22329759). Austinol can be further modified to dehydroaustinol which forms a diffusible complex with diorcinol that initiates conidiation (PubMed:22234162, PubMed:22329759).
 ausB ELISA Kit
 ausB Recombinant
 ausB Antibody
 AN8379 ELISA Kit
 AN8379 Recombinant
 AN8379 Antibody
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FAD-binding monooxygenase ausC

 FAD-binding monooxygenase ausC ELISA Kit
 FAD-binding monooxygenase ausC Recombinant
 FAD-binding monooxygenase ausC Antibody
Also known as FAD-binding monooxygenase ausC (Austinol synthesis protein C).
FAD-binding monooxygenase; part of the gene cluster A that mediates the biosynthesis of austinol and dehydroaustinol, two fungal meroterpenoids (PubMed:22329759). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (PubMed:22329759). 3,5-dimethylorsellinic acid
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is then prenylated by the polyprenyl transferase ausN (PubMed:22329759). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A (PubMed:22329759). Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE (PubMed:22329759, PubMed:23865690). Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4 (PubMed:22329759). The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide (PubMed:22329759). Finally, the cytochrome P450 monooxygenase ausG modifies austinolide to austinol (PubMed:22329759). Austinol can be further modified to dehydroaustinol which forms a diffusible complex with diorcinol that initiates conidiation (PubMed:22234162, PubMed:22329759).
 ausC ELISA Kit
 ausC Recombinant
 ausC Antibody
 AN8381 ELISA Kit
 AN8381 Recombinant
 AN8381 Antibody
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FAD-binding monooxygenase hmp7

 FAD-binding monooxygenase hmp7 ELISA Kit
 FAD-binding monooxygenase hmp7 Recombinant
 FAD-binding monooxygenase hmp7 Antibody
Also known as FAD-binding monooxygenase hmp7 (FMO hmp7) (Hypothemycin biosynthesis cluster protein hpm7).
FAD-binding monooxygenase; part of the gene cluster that mediates the biosynthesis of hypothemycin, a resorcylic acid lactone (RAL) that irreversibly inhibits a subset of protein kinases with a conserved cysteine in the ATP binding site such as human ERK2 (PubMed:18567690). The first step i
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s performed by both PKSs hmp3 and hmp8 and leads to the production of 7',8'-dehydrozearalenol (DHZ) (PubMed:18567690, PubMed:20222707). The highly reducing PKS hpm8 synthesizes the reduced hexaketide (7S,11S,2E,8E)-7,11-dihydroxy-dodeca-2,8-dienoate, which is transferred downstream to the non-reducing PKS hpm3 (PubMed:20222707). Hpm3 then extends the reduced hexaketide to a nonaketide, after which regioselective cyclization and macrolactonization affords DHZ (PubMed:20222707). The next step is the conversion of DHZ into aigialomycin C and is performed by the O-methyltransferase hmp5, the FAD-binding monooxygenase hmp7, and the cytochrome P450 monooxygenase hmp1 (PubMed:18567690). The wide substrate tolerance of the hmp5 and hmp7 implies that the reactions from DHZ to aigialomycin C can occur in any order (PubMed:18567690). The steps from aigialomycin C to hypothemycin are less well established (PubMed:18567690). The FAD-linked oxidoreductase hmp9 presumably catalyzes oxidation of the C-6' hydroxyl to a ketone (PubMed:18567690). The timing of this oxidation is important, since the resulting enone functional group is a Michael acceptor that can react spontaneously with glutathione, an abundant metabolite in fungal cells (PubMed:18567690). The glutathione S-transferase hmp2 catalyzes cis-trans isomerization of the 7',8' double bond with equilibrium favoring the trans isomer (PubMed:18567690). The hpm6-encoded transporter might preferentially pump hypothemycin out of the cell relative to the trans isomer aigialomycin A. The cis-to-trans isomerization may be coupled with C-4' hydroxylation, since all known hypothemycin analogs containing the enone functional group also have hydroxyl groups at both C-4' and C-5' (PubMed:18567690).
 hpm7 ELISA Kit
 hpm7 Recombinant
 hpm7 Antibody
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FAD-binding monooxygenase trt3

 FAD-binding monooxygenase trt3 ELISA Kit
 FAD-binding monooxygenase trt3 Recombinant
 FAD-binding monooxygenase trt3 Antibody
Also known as FAD-binding monooxygenase trt3 (Terretonin synthesis protein 3).
FAD-binding monooxygenase; part of the gene cluster that mediates the biosynthesis of terretonin, a fungal meroterpenoid that acts as a mycotoxin (PubMed:22549923, PubMed:23116177, PubMed:25671343). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase trt4 (P
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ubMed:22549923, PubMed:23116177). DMOA is then prenylated into farnesyl-DMOA by the polyprenyl transferase trt2 (PubMed:22549923, PubMed:22782788, PubMed:23116177). Methylation by the methyltransferase trt5 then leads to farnesyl-DMOA methyl ester which is further subject to epoxidation by the FAD-dependent monooxygenase trt8 to yield epoxyfarnesyl-DMOA methyl ester (PubMed:22549923, PubMed:22782788, PubMed:23116177). Cyclization of epoxyfarnesyl-DMOA methyl ester by the terpene cyclase trt1 leads to a tetracycle intermediate which is in turn converted to preterretonin (PubMed:22549923, PubMed:22782788, PubMed:23116177). Dehydrogenase trt9 comes next to transform preterretonin to preterrenoid (PubMed:22549923, PubMed:23116177). The FAD-dependent monooxygenase trt3 is then required for the C-hydroxylation at C16 of preterrenoid to yield terrenoid (PubMed:22549923, PubMed:23116177). The cytochrome P450 trt6 catalyzes three successive oxidations to transform terrenoid into an unstable intermediate, which then undergoes the D-ring expansion and unusual rearrangement of the methoxy group to afford the core skeleton of terretonin (PubMed:25671343). This unprecedented rearrangement is catalyzed by the isomerase trt14 (PubMed:25671343). Finally, the nonheme iron-dependent dioxygenase trt7 accomplishes the last two oxidation reactions steps to complete the biosynthesis of terretonin (PubMed:25671343). Terretonin C is produced via spontaneous decarboxylation of the terretonin precursor (PubMed:23116177). Another shunt product of the terretonin biosynthesis is dihydrofarnesyl-DMOA, derived from epoxyfarnesyl-DMOA through hydrolysis of the epoxide (PubMed:22549923, PubMed:22782788, PubMed:23116177).
 trt3 ELISA Kit
 trt3 Recombinant
 trt3 Antibody
 ATEG_10079 ELISA Kit
 ATEG_10079 Recombinant
 ATEG_10079 Antibody
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