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FAD-dependent monooxygenase

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FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of asperfuranone, a probable antitumor agent .

Below are the list of possible FAD-dependent 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-dependent monooxygenase afoD

 FAD-dependent monooxygenase afoD ELISA Kit
 FAD-dependent monooxygenase afoD Recombinant
 FAD-dependent monooxygenase afoD Antibody
Also known as FAD-dependent monooxygenase afoD (Asperfuranone biosynthesis protein D).
FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of asperfuranone, a probable antitumor agent (PubMed:19199437). The polyketide synthase afoG is responsible for producing the 3,5-dimethyloctadienone moiety from acetyl-CoA, three malonyl-CoA, and two S-adenosyl methionines (
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SAM) (PubMed:19199437). The 3,5-dimethyloctadienone moiety is then loaded onto the SAT domain of afoE and extended with four malonyl-CoA and one SAM, which leads to the formation of 2,4-dihydroxy-6-(5,7-dimethyl-2-oxo-trans-3-trans-5-nonadienyl)-3-methylbenzaldehyde (compound 2) after reductive release and aldol condensation (PubMed:19199437). AfoD is the next enzyme in the biosynthesis sequence and hydroxylates the side chain at the benzylic position of compound 2 (PubMed:19199437). After benzylic hydroxylation, a furan ring is formed after five-member ring hemiacetal formation and water elimination (PubMed:19199437). AfoF and afoC are proposed to oxidize the R-diketone proton and to reduce the unconjugated carbonyl group, respectively, to generate asperfuranone (PubMed:19199437). Since no intermediates could be isolated from afoF and afoC deletants, the sequence of these two enzymes is not fully understood (PubMed:19199437). Moreover, since afoC deletant still produces a small amount of asperfuranone, other endogenous oxidoreductases might catalyze the same reaction with much less efficiency (PubMed:19199437).
 afoD ELISA Kit
 afoD Recombinant
 afoD Antibody
 AN1033 ELISA Kit
 AN1033 Recombinant
 AN1033 Antibody
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FAD-dependent monooxygenase andE

 FAD-dependent monooxygenase andE ELISA Kit
 FAD-dependent monooxygenase andE Recombinant
 FAD-dependent monooxygenase andE Antibody
Also known as FAD-dependent monooxygenase andE (Anditomin synthesis protein E).
FAD-dependent 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
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compound 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).
 andE ELISA Kit
 andE Recombinant
 andE Antibody
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FAD-dependent monooxygenase aptC

 FAD-dependent monooxygenase aptC ELISA Kit
 FAD-dependent monooxygenase aptC Recombinant
 FAD-dependent monooxygenase aptC Antibody
Also known as FAD-dependent monooxygenase aptC (Asperthecin synthesis protein C).
FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of asperthecin, an anthraquinone pigment (PubMed:18978088, PubMed:21866960). Polyketide synthase (PKS) aptA catalyzes the formation of the aromatic polyketide from acetyl coenzyme A and seven malonyl coenzyme A molecules (PubMed:1
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8978088). Polyketide is subsequently hydrolyzed by the action of the hydrolase aptB into endocrocin-9-anthrone (PubMed:18978088). Endocrocin-9-anthrone is then oxidized into endocrocin by the monooxygenase aptC (PubMed:18978088). Endocrocin is likely to decarboxylate spontaneously to form emodin which explains why there is no decarboxylase in the asperthecin biosynthesis cluster (PubMed:18978088). Finally, aptC or another endogenous oxygenase catalyzes additional oxidation steps to form asperthecin (PubMed:18978088).
 aspC ELISA Kit
 aspC Recombinant
 aspC Antibody
 AN6002.2 ELISA Kit
 AN6002.2 Recombinant
 AN6002.2 Antibody
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FAD-dependent monooxygenase asqG

 FAD-dependent monooxygenase asqG ELISA Kit
 FAD-dependent monooxygenase asqG Recombinant
 FAD-dependent monooxygenase asqG Antibody
Also known as FAD-dependent monooxygenase asqG (4'-methoxyviridicatin/aspoquinolone biosynthesis cluster protein asqG) (Aspoquinolone biosynthesis protein G).
FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the aspoquinolone mycotoxins (PubMed:25251934). The first stage is catalyzed by the nonribosomal pepdide synthetase asqK that condenses anthranilic ac
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id and O-methyl-L-tyrosine to produce 4'-methoxycyclopeptin (PubMed:25251934). AsqK is also able to use anthranilic acid and L-phenylalanine as substrates to produce cyclopeptin, but at a tenfold lower rate (PubMed:25251934). 4'-methoxycyclopeptin is then converted to 4'-methoxydehydrocyclopeptin by the ketoglutarate-dependent dioxygenase asqJ through dehydrogenation to form a double bond between C-alpha and C-beta of the O-methyltyrosine side chain (PubMed:25251934). AsqJ also converts its first product 4'-methoxydehydrocyclopeptin to 4'-methoxycyclopenin (PubMed:25251934). AsqJ is a very unique dioxygenase which is capable of catalyzing radical-mediated dehydrogenation and epoxidation reactions sequentially on a 6,7-benzo-diazepinedione substrate in the 4'-methoxyviridicatin biosynthetic pathway (PubMed:25251934). The following conversion of 4'-methoxycyclopenin into 4'-methoxyviridicatin proceeds non-enzymatically (PubMed:25251934). AsqJ is also capable of converting cyclopeptin into dehydrocyclopeptin and cyclopenin in a sequential fashion (PubMed:25251934). Cyclopenin can be converted into viridicatin non-enzymatically (PubMed:25251934). 4'-methoxyviridicatin likely acts as a precursor of quinolone natural products, such as aspoquinolones, peniprequinolones, penigequinolones, and yaequinolones (PubMed:25251934). Further characterization of the remaining genes in the cluster has still to be done to determine the exact identity of quinolone products this cluster is responsible for biosynthesizing (PubMed:25251934).
 asqG ELISA Kit
 asqG Recombinant
 asqG Antibody
 AN9230 ELISA Kit
 AN9230 Recombinant
 AN9230 Antibody
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FAD-dependent monooxygenase atmM

 FAD-dependent monooxygenase atmM ELISA Kit
 FAD-dependent monooxygenase atmM Recombinant
 FAD-dependent monooxygenase atmM Antibody
Also known as FAD-dependent monooxygenase atmM (Aflatrem synthesis protein M).
FAD-dependent monooxygenase; part of the ATM1 gene cluster that mediates the biosynthesis of aflatrem, a tremorgenic mycotoxin with acute neurotoxic effects (PubMed:15528556, PubMed:19801473, PubMed:2867895). Synthesis of geranylgeranyl diphosphate (GGPP) by AtmG (a GGPP synthase) precedes condensation of GGPP with i
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ndole 3-glycerol phosphate, followed by epoxidation and cyclization by AtmM (a FAD-dependent monooxygenase) and AtmC (a prenyltransferase) to produce paspaline (PubMed:19801473). AtmB is also essential for paspaline production, but its exact role has not been identified yet (PubMed:19801473). AtmP, a cytochrome P450 monooxygenase, subsequently converts paspaline to 13-desoxypaxilline via PC-M6 by removal of the C-30 methyl group and oxidation at C-10 (PubMed:19801473). AtmQ, a cytochrome P450 monooxygenase, then catalyzes the oxidation of 13-desoxypaxilline, first at C-7 to produce paspalicine and then at C-13 to form paspalinine (PubMed:19801473). Finally, AtmD prenylates paspalinine to form aflatrem (PubMed:19801473).
 atmM ELISA Kit
 atmM Recombinant
 atmM Antibody
 AF113 ELISA Kit
 AF113 Recombinant
 AF113 Antibody
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FAD-dependent monooxygenase ausM

 FAD-dependent monooxygenase ausM ELISA Kit
 FAD-dependent monooxygenase ausM Recombinant
 FAD-dependent monooxygenase ausM Antibody
Also known as FAD-dependent monooxygenase ausM (Austinol synthesis protein M).
FAD-dependent monooxygenase; part of the gene cluster B 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 a
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cid 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).
 ausM ELISA Kit
 ausM Recombinant
 ausM Antibody
 AN11206 ELISA Kit
 AN11206 Recombinant
 AN11206 Antibody
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FAD-dependent monooxygenase azaH

 FAD-dependent monooxygenase azaH ELISA Kit
 FAD-dependent monooxygenase azaH Recombinant
 FAD-dependent monooxygenase azaH Antibody
Also known as FAD-dependent monooxygenase azaH (Azaphilone biosynthesis cluster protein azaH).
FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of azaphilones, a class of fungal metabolites characterized by a highly oxygenated pyrano-quinone bicyclic core and exhibiting a broad range of bioactivities (PubMed:22921072). In the first step, the non-reducing poly
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ketide synthase azaA forms the hexaketide precursor from successive condensations of five malonyl-CoA units, presumably with a simple acetyl-CoA starter unit (PubMed:22921072). The reactive polyketide chain then undergoes a PT-mediated C2-C7 cyclization to afford the aromatic ring and is eventually released as an aldehyde through the R-domain (PubMed:22921072). The putative ketoreductase azaE is proposed to catalyze the reduction of the terminal ketone resulting in the early culture product FK17-P2a (PubMed:22921072). The monooxygenase azaH was demonstrated to be the only enzyme required to convert FK17-P2a to azanigerone E (PubMed:22921072). AzaH first hydroxylates the benzaldehyde intermediate FK17-P2a at C4, which triggers the formation of the pyran-ring to afford azanigerone E (PubMed:22921072). In parallel, the 2,4-dimethylhexanoyl chain is synthesized by the HR-PKS azaB and is proposed to be transferred to the C4-hydroxyl of azanigerone E by the acyltransferase azaD directly from the ACP domain of azaB (PubMed:22921072). Alternatively, the 2,4-dimethyl-hexanoyl chain may be offloaded from the HR-PKS as a carboxylic acid and converted to an acyl-CoA by azaF (PubMed:22921072). The resulting acyl-CoA molecule could then be taken up as a substrate by AzaD to form azanigerone B (PubMed:22921072). To yield the carboxylic acid substituent in azanigerone A, the hydroxypropyl side chain of azanigerone B would need to undergo a C-C oxidative cleavage catalyzed by cytochrome P450 AzaI (PubMed:22921072). AzaI is proposed to act on a vicinal diol that leads to a C-C bond scission either through an alkoxyradical intermediate or a peroxy complex (PubMed:22921072). In the biosynthesis of azanigerone A, azanigerone B first undergoes hydroxylation at C10, possibly catalyzed by one of the two FAD-dependent monooxygenases encoded in the cluster, azaG or azaL, resulting in the vicinal diol azanigerone C (PubMed:22921072). Oxidative cleavage of azanigerone C by azaI would yield the corresponding aldehyde derivative of azanigerone A (PubMed:22921072). Finally, the dehydrogenase azaJ is proposed to convert the aldehyde functional group into the carboxylic acid, completing the conversion from azanigerone B to azanigerone A (PubMed:22921072). Alternatively, the oxidation of aldehyde to carboxylic acid may be catalyzed by the same P450 enzyme azaI via consecutive oxidation or by endogenous alcohol dehydrogenase (PubMed:22921072).
 azaH ELISA Kit
 azaH Recombinant
 azaH Antibody
 ASPNIDRAFT_188800 ELISA Kit
 ASPNIDRAFT_188800 Recombinant
 ASPNIDRAFT_188800 Antibody
Table BarTOPTable Bar
 

FAD-dependent monooxygenase bik2

 FAD-dependent monooxygenase bik2 ELISA Kit
 FAD-dependent monooxygenase bik2 Recombinant
 FAD-dependent monooxygenase bik2 Antibody
Also known as FAD-dependent monooxygenase bik2 (Bikaverin biosynthesis protein 2).
FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of bikaverin, a red pigment also considered as a mycotoxin (PubMed:19400779). The first stage is catalyzed by the polyketide synthase bik1, which catalyzes the formation of the intermediate SMA76a also knowm as pre-bikaverin (Pub
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Med:19400779). FAD-dependent monooxygenase bik2 might then be responsible for the oxidation of pre-bikaverin to oxo-pre-bikaverin which is in turn methylated by the O-methyltransferase bik3 to me-oxo-pre-bikaverin (PubMed:26382642). A further cycle of oxydation and methylation by bik2 and bik3 leads to the final product of bikaverin, via a nor-bikaverin intermediate (PubMed:19400779, PubMed:26382642).
 bik2 ELISA Kit
 bik2 Recombinant
 bik2 Antibody
 FFUJ_06743 ELISA Kit
 FFUJ_06743 Recombinant
 FFUJ_06743 Antibody
Table BarTOPTable Bar
 

FAD-dependent monooxygenase ctvC

 FAD-dependent monooxygenase ctvC ELISA Kit
 FAD-dependent monooxygenase ctvC Recombinant
 FAD-dependent monooxygenase ctvC Antibody
Also known as FAD-dependent monooxygenase ctvC (Citreoviridin biosynthesis protein C).
FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of citreoviridin, an inhibitor of the of F1-ATPase beta-subunit (PubMed:26954888). The HR-PKS ctvA accepts acetyl-CoA as the starter unit and catalyzes eight iterations of malonyl-CoA extension and four iterations of SAM-depe
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ndent methylation at C4, C12, C14, and C16 (PubMed:26954888). The KR and DH domains selectively act on the first six iterations to generate the hexaene chain (PubMed:26954888). In the last three iterations, the KR and DH domains terminate their functions to yield a beta,delta-diketo ester moiety, which then undergoes intramolecular cyclization to yield an alpha-pyrone intermediate (PubMed:26954888). Subsequently, ctvB methylates the alpha-pyrone hydroxyl group to generate citreomontanin (PubMed:26954888). In order to form the tetrahydrofuran ring with the correct stereochemistry, the terminal alkenes of citreomontanin need to undergo isomerization to yield a (17Z)-hexaene, a step that could be catalyzed by ctvC (PubMed:26954888). The (17Z)-hexaene then undergoes bisepoxidation by ctvC to form a (17R,16R,15S,14R)-bisepoxide moiety (PubMed:26954888). Lastly, ctvD acts as a regioselective hydrolase to form the tetrahydrofuran ring with the substituents in the correct absolute configuration, completing the biosynthesis of citreoviridin (PubMed:26954888).
 ctvC ELISA Kit
 ctvC Recombinant
 ctvC Antibody
 ATEG_09620 ELISA Kit
 ATEG_09620 Recombinant
 ATEG_09620 Antibody
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FAD-dependent monooxygenase mdpD

 FAD-dependent monooxygenase mdpD ELISA Kit
 FAD-dependent monooxygenase mdpD Recombinant
 FAD-dependent monooxygenase mdpD Antibody
Also known as FAD-dependent monooxygenase mdpD (Monodictyphenone synthesis protein D).
FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of monodictyphenone, a prenyl xanthone derivative (PubMed:20139316, PubMed:21351751). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) mdpG (PubMed:20139316). The atrochrysone c
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arboxyl ACP thioesterase mdpF then breaks the thioester bond and releases the atrochrysone carboxylic acid from gedC (PubMed:20139316). The atrochrysone carboxylic acid is then converted to atrochrysone which is further transformed into emodin anthrone (PubMed:20139316). The next step is performed by the anthrone oxygenase mdpH that catalyzes the oxidation of emodinanthrone to emodin (). Emodin is further mofified to yield monodictyphenone via several steps involving by mdpB, mdpC mdpJ, mdpK and mdpL (PubMed:20139316, PubMed:21351751).
 mdpD ELISA Kit
 mdpD Recombinant
 mdpD Antibody
 AN0147 ELISA Kit
 AN0147 Recombinant
 AN0147 Antibody
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FAD-dependent monooxygenase nscC

 FAD-dependent monooxygenase nscC ELISA Kit
 FAD-dependent monooxygenase nscC Recombinant
 FAD-dependent monooxygenase nscC Antibody
Also known as FAD-dependent monooxygenase nscC (Neosartoricin B biosynthesis protein C).
FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of neosartoricin B, a prenylated anthracenone that probably exhibits T-cell antiproliferative activity, suggestive of a physiological role as an immunosuppressive agent (PubMed:23758576). The non-reducing polyketide synthas
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e nscA probably synthesizes and cyclizes the decaketide backbone (). The hydrolase nscB then mediates the product release through hydrolysis followed by spontaneous decarboxylation (). The prenyltransferase nscD catalyzes the addition of the dimethylallyl group to the aromatic C5 (). The FAD-dependent monooxygenase nscC is then responsible for the stereospecific hydroxylation at C2 (). Neosartoricin B can be converted into two additional compounds neosartoricins C and D (). Neosartoricin C is a spirocyclic compound that is cyclized through the attack of C3 hydroxyl on C14, followed by dehydration (). On the other hand, neosartoricin D is a further cyclized compound in which attack of C2 on C14 in neosartoricin C results in the formation of the acetal-containing dioxabicyclo-octanone ring (). Both of these compounds are novel and possibly represent related metabolites of the gene cluster ().
 nscC ELISA Kit
 nscC Recombinant
 nscC Antibody
 MGYG_06590 ELISA Kit
 MGYG_06590 Recombinant
 MGYG_06590 Antibody
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FAD-dependent monooxygenase paxM

 FAD-dependent monooxygenase paxM ELISA Kit
 FAD-dependent monooxygenase paxM Recombinant
 FAD-dependent monooxygenase paxM Antibody
Also known as FAD-dependent monooxygenase paxM (Paxilline synthesis protein M).
FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of paxilline, a mycotoxin that acts as an inhibitor of mammalian maxi-K channels (PubMed:11169115, PubMed:23949005, PubMed:16494875). PaxG, the geranylgeranyl diphosphate (GGPP) synthase is proposed to catalyze the first step in pax
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illine biosynthesis (PubMed:23949005, PubMed:16494875). Condensation of indole-3-glycerol phosphate with GGPP by paxC then forms 3-geranylgeranylindole (3-GGI), followed by epoxidation and cyclization of this intermediate (by paxM and paxB) to form paspaline (PubMed:23949005, PubMed:16494875). Paspaline is subsequently converted to 13-desoxypaxilline by paxP, the latter being then converted to paxilline by paxQ (PubMed:23949005). Finally paxilline can be mono- and di-prenylated by paxD (PubMed:23949005).
 paxM ELISA Kit
 paxM Recombinant
 paxM Antibody
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FAD-dependent monooxygenase pyr5

 FAD-dependent monooxygenase pyr5 ELISA Kit
 FAD-dependent monooxygenase pyr5 Recombinant
 FAD-dependent monooxygenase pyr5 Antibody
Also known as FAD-dependent monooxygenase pyr5 (Pyripyropene synthesis protein 5).
FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of pyripyropene A, a specific human acyl-coenzyme A:cholesterol acyltransferase 2 inhibitor (PubMed:20861902). The first step of the pathway is the synthesis of nicotinyl-CoA from nicotinic acid by the nicotinic acid-CoA ligase p
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yr1 (PubMed:20861902). Nicotinyl-CoA is then a substrate of polyketide synthase pyr2 to produce 4-hydroxy-6-(3-pyridinyl)-2H-pyran-2-one (HPPO) which is further prenylated by the polyprenyl transferase pyr6 to yield farnesyl-HPPO (PubMed:20861902). The next steps consist of an epoxidation of farnesyl-HPPO to epoxyfarnesyl-HPPO by FAD-dependent monooxygenase pyr5 and a cyclization of the terpenoid portion by the terpene cyclase pyr4 to yield deacetyl-pyripyropene E (PubMed:20861902). The 2 cytochrome P450 monooxygenases pyr3 and pyr9, and the 2 acetyltransferases pyr7 and pyr8 are involved in the conversion of deacetyl-pyripyropene E into pyripyropene A through several cycles of oxidation and acetylation steps (PubMed:20861902). Pyr7 acetylates deacetyl-pyripyropene E to pyripyropene E which is oxidized to 11-deacetyl-pyripyropene O by pyr3, which is in turn acetylated into pyripyropene O by pyr8 (PubMed:21224862, PubMed:26019565). Pyripyropene O is then oxidized to deacetyl-pyripyropene A by pyr9 (PubMed:21224862). Deacetyl-pyripyropene A is finally acetylated to pyripyropene A by pyr8 (PubMed:26019565).
 pyr5 ELISA Kit
 pyr5 Recombinant
 pyr5 Antibody
 AFUA_6G13970 ELISA Kit
 AFUA_6G13970 Recombinant
 AFUA_6G13970 Antibody
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FAD-dependent monooxygenase roqM

 FAD-dependent monooxygenase roqM ELISA Kit
 FAD-dependent monooxygenase roqM Recombinant
 FAD-dependent monooxygenase roqM Antibody
Also known as FAD-dependent monooxygenase roqM (Roquefortine/meleagrin synthesis protein M).
FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the mycotoxin meleagrin (PubMed:22118684, PubMed:23776469). The first stage is catalyzed by the dipeptide synthase roqA which condenses histidine and tryptophan to produce histidyltryptophanyldiketopiperazine (HTD) (
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PubMed:22118684, PubMed:23776469). HTD is then converted to roquefortine C through two possible pathways (PubMed:23776469). In the first pathway, prenyltransferase roqD transforms HTD to the intermediate roquefortine D, which is in turn converted to roquefortine C by the cytochrome P450 monooxygenase roqR (PubMed:23776469). In the second pathway, HTD is first converted to the intermediate dehydrohistidyltryptophanyldi-ketopiperazine (DHTD) by roqR which is then prenylated by roqD to form roquefortine C (PubMed:23776469). Roquefortine C can be further transformed to meleagrin via three more reactions including oxydation to glandicolin A by roqM, which is further reduced to glandicoline B by roqO (PubMed:23776469). Finally, glandicoline B is converted to meleagrin by the glandicoline B O-methyltransferase roqN (PubMed:22118684, PubMed:23776469). More studies identified further branching and additional metabolites produced by the roquefortine/meleagrin cluster, including roquefortine F, roquefortine L, roquefortine M, roquefortine N and neoxaline (PubMed:24225953).
 roqM ELISA Kit
 roqM Recombinant
 roqM Antibody
 Pc21g15460 ELISA Kit
 Pc21g15460 Recombinant
 Pc21g15460 Antibody
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FAD-dependent monooxygenase terC

 FAD-dependent monooxygenase terC ELISA Kit
 FAD-dependent monooxygenase terC Recombinant
 FAD-dependent monooxygenase terC Antibody
Also known as FAD-dependent monooxygenase terC (Terrein biosynthesis cluster protein terC).
FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of terrein, a fungal metabolite with ecological, antimicrobial, antiproliferative, and antioxidative activities (PubMed:24816227). The first step in the pathway is performed by the polyketide synthase terA that produces
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4-hydroxy-6-methylpyranon (4-HMP), orsellinic acid (OA), and 2,3-dehydro-6-hydroxymellein (2,3-dehydro-6-HM) by condensing acetyl-CoA with two, three, or four malonyl-CoA units, respectively (PubMed:24816227). 4-HMP and OA are not pathway intermediates, but are rather shunt or side products (PubMed:24816227). 2,3-dehydro-6-HM is further converted to 6-hydroxymellein (6-HM) by the 6-hydroxymellein synthase terB (PubMed:24816227). The monooxygenases terC and terD, the multicopper oxidase terE and the Kelch-like protein terF are then involved in the transformation of 6-HM to terrein (PubMed:24816227). Even if they are co-regulated with the other terrein cluster genes, terH and terI seem to be dispensable for terrein production; whereas one or both of the 2 transporters terG or terJ are probably required for efficient secretion of metabolites (PubMed:24816227).
 terC ELISA Kit
 terC Recombinant
 terC Antibody
 ATEG_00143 ELISA Kit
 ATEG_00143 Recombinant
 ATEG_00143 Antibody
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FAD-dependent monooxygenase terD

 FAD-dependent monooxygenase terD ELISA Kit
 FAD-dependent monooxygenase terD Recombinant
 FAD-dependent monooxygenase terD Antibody
Also known as FAD-dependent monooxygenase terD (Terrein biosynthesis cluster protein terD).
FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of terrein, a fungal metabolite with ecological, antimicrobial, antiproliferative, and antioxidative activities (PubMed:24816227). The first step in the pathway is performed by the polyketide synthase terA that produces
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4-hydroxy-6-methylpyranon (4-HMP), orsellinic acid (OA), and 2,3-dehydro-6-hydroxymellein (2,3-dehydro-6-HM) by condensing acetyl-CoA with two, three, or four malonyl-CoA units, respectively (PubMed:24816227). 4-HMP and OA are not pathway intermediates, but are rather shunt or side products (PubMed:24816227). 2,3-dehydro-6-HM is further converted to 6-hydroxymellein (6-HM) by the 6-hydroxymellein synthase terB (PubMed:24816227). The monooxygenases terC and terD, the multicopper oxidase terE and the Kelch-like protein terF are then involved in the transformation of 6-HM to terrein (PubMed:24816227). Even if they are co-regulated with the other terrein cluster genes, terH and terI seem to be dispensable for terrein production; whereas one or both of the 2 transporters terG and terJ are probably required for efficient secretion of metabolites (PubMed:24816227).
 terD ELISA Kit
 terD Recombinant
 terD Antibody
 ATEG_00142 ELISA Kit
 ATEG_00142 Recombinant
 ATEG_00142 Antibody
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FAD-dependent monooxygenase tropB

 FAD-dependent monooxygenase tropB ELISA Kit
 FAD-dependent monooxygenase tropB Recombinant
 FAD-dependent monooxygenase tropB Antibody
Also known as FAD-dependent monooxygenase tropB (Tropolone synthesis protein B).
FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the tropolone class of fungal maleic anhydrides (PubMed:22508998, PubMed:24863423). The pathway begins with the synthesis of 3-methylorcinaldehyde by the non-reducing polyketide synthase (PKS) tropA (PubMed:22508998). 3-methylorcinaldehyde is the substrate for the FAD-dependent monooxygenase tropB to yield a dearomatized hydroxycyclohexadione (PubMed:22508998, PubMed:24863423). The 2-oxoglutarate-dependent dioxygenase tropC
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then performs the oxidative ring expansion to provide the first tropolone metabolite stipitaldehyde (PubMed:22508998, PubMed:24863423). Trop D converts stipitaldehyde into stipitacetal which is in turn converted to stipitalide by the short-chain dehydrogenase/reductase tropE (PubMed:24863423). The next steps involve tropF, tropG, tropH, tropI and tropJ to form successive tropolone maleic anhydrides including stipitaldehydic, stipitatonic and stipitatic acids (PubMed:24863423).
 tropB ELISA Kit
 tropB Recombinant
 tropB Antibody
 tsL1 ELISA Kit
 tsL1 Recombinant
 tsL1 Antibody
 TSTA_117740 ELISA Kit
 TSTA_117740 Recombinant
 TSTA_117740 Antibody
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FAD-dependent monooxygenase trt8

 FAD-dependent monooxygenase trt8 ELISA Kit
 FAD-dependent monooxygenase trt8 Recombinant
 FAD-dependent monooxygenase trt8 Antibody
Also known as FAD-dependent monooxygenase trt8 (Terretonin synthesis protein 8).
FAD-dependent 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 trt
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4 (PubMed: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).
 trt8 ELISA Kit
 trt8 Recombinant
 trt8 Antibody
 ATEG_10085 ELISA Kit
 ATEG_10085 Recombinant
 ATEG_10085 Antibody
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FAD-dependent monooxygenase vrtH

 FAD-dependent monooxygenase vrtH ELISA Kit
 FAD-dependent monooxygenase vrtH Recombinant
 FAD-dependent monooxygenase vrtH Antibody
Also known as FAD-dependent monooxygenase vrtH (Viridicatumtoxin synthesis protein H).
FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of viridicatumtoxin, a tetracycline-like fungal meroterpenoid with a unique, fused spirobicyclic ring system (PubMed:20534346). The first step of the pathway is the production of the malonamoyl-CoA starter unit for the polyke
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tide synthase vrtA (PubMed:20534346). The aldolase vrtJ may be involved in the synthesis of the malonamate substrate for malonamoyl-CoA synthetase vrtB (PubMed:20534346). The polyketide synthase vrtA then may utilize the malonamoyl-CoA starter unit, followed by sequential condensation of eight malonyl-CoA units to form the polyketide backbone (PubMed:20534346). The cyclization of the last ring could be mediated by the lactamase-like protein vrtG (PubMed:20534346). The proposed post-PKS tailoring steps are an hydroxylation at C5 catalyzed the cytochrome P450 monooxygenase vrtE, an hydroxylation at C12a catalyzed by VrtH and/or VrtI, and an O-methylation by the O-methyltransferase vrtF (PubMed:20534346, PubMed:24161266). VrtC is then proposed to catalyze the transfer of a geranyl group synthesized by vrtD to the aromatic C ring of the tetracyclic polyketide intermediate of viridicatumtoxin to yield previridicatumtoxin (PubMed:20534346). Finally, the cytochrome P450 monooxygenase vrtK catalyzes the spirocyclization of the geranyl moeity of previridicatumtoxin to afford viridicatumtoxin (PubMed:24161266).
 vrtH ELISA Kit
 vrtH Recombinant
 vrtH Antibody
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FAD-dependent monooxygenase yanF

 FAD-dependent monooxygenase yanF ELISA Kit
 FAD-dependent monooxygenase yanF Recombinant
 FAD-dependent monooxygenase yanF Antibody
Also known as FAD-dependent monooxygenase yanF (Yanuthone D synthesis protein F).
FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of yanuthone D, a fungal isoprenoid epoxycyclohexenone that acts as an antibiotic against fungi and bacteria (PubMed:24684908). The first step of the pathway is the synthesis of 6-methylsalicylic acid (6-MSA) by the polyketide syn
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thase yanA (PubMed:24684908). 6-MSA is then converted to m-cresol by the decarboxylase yanB (PubMed:24684908). The cytochrome P450 monooxygenase yanC then catalyzes the oxidation of m-cresol to toluquinol (PubMed:24684908). Epoxidation of toluquinol is then performed by the short chain dehydrogenase yanD, with the help of yanE, and a further prenylated by yanG leads to 7-deacetoxyyanuthone A (PubMed:24684908). The next step is the hydroxylation of C-22 of 7-deacetoxyyanuthone A by the cytochrome P450 monooxygenase yanH to yield 22-deacetylyanuthone A (PubMed:24684908). O-Mevalon transferase yanI then attaches mevalon to the hydroxyl group of 22-deacetylyanuthone A to produce yanuthone E (PubMed:24684908). Finally, the FAD-dependent monooxygenase yanF oxidizes the hydroxyl group at C15 of yanuthone E to form yanuthone D (PubMed:24684908). Furthermore, several branching points in the pathway lead to the production of yanuthones F and G from 7-deacetoxyyanuthone A; yanuthones H and I from 22-deacetylyanuthone A; and yanuthone J from yanuthone E (PubMed:24684908).
 yanF ELISA Kit
 yanF Recombinant
 yanF Antibody
 ASPNIDRAFT_44970 ELISA Kit
 ASPNIDRAFT_44970 Recombinant
 ASPNIDRAFT_44970 Antibody
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Proteins Root Name Listing
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