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FAD-linked oxidoreductase

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

Below are the list of possible FAD-linked oxidoreductase 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-linked oxidoreductase afoF

 FAD-linked oxidoreductase afoF ELISA Kit
 FAD-linked oxidoreductase afoF Recombinant
 FAD-linked oxidoreductase afoF Antibody
Also known as FAD-linked oxidoreductase afoF (Asperfuranone biosynthesis protein B).
FAD-linked oxidoreductase; 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 (SAM)
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(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).
 afoF ELISA Kit
 afoF Recombinant
 afoF Antibody
 AN1035 ELISA Kit
 AN1035 Recombinant
 AN1035 Antibody
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FAD-linked oxidoreductase apf9

 FAD-linked oxidoreductase apf9 ELISA Kit
 FAD-linked oxidoreductase apf9 Recombinant
 FAD-linked oxidoreductase apf9 Antibody
Also known as FAD-linked oxidoreductase apf9 (Apicidin F synthesis protein 9).
FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of the cyclic tetrapeptide apicidin F (APF) (PubMed:25058475). The non-ribosomal peptide synthetase apf1 incorporates four different amino acids to produce apicidin F: L-phenylalanine, D-pipecolic acid (D-pip), N-methoxy-L-tryptophan a
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nd L-2-aminooctanedioic acid (PubMed:25058475). L-Phenylalanine is the only proteinogenic amino acid directly used by apf1 (PubMed:24195442, PubMed:25058475). The 3 other apf1 substrates are non-proteinogenic and have to be modified by other enzymes of the cluster (PubMed:25058475). Lysine is converted to delta-1-pyrroline-5-carboxylate (P5C) which is reduced to L-pipecolic acid (L-pip) by apf3 (PubMed:25058475). L-pip is epimerized to D-pip, probably by apf1 activity, prior to incorporation (PubMed:25058475). L-Tryptophan is N-oxidyzed by one of the cytochrome P450 monooxygenases (apf7 or apf8), and further methylated at the hydroxy group by the O-methyltransferase apf6 to yield N-methoxy-L-tryptophan (PubMed:25058475). The synthesis of the fourth apf1 substrate is more complex (PubMed:25058475). The fatty acid synthase apf5 is involved in the synthesis of the octanoic acid backbone of L-2-aminooctanedioic acid by fixing one acetyl-CoA unit and three malonyl-CoA units (PubMed:25058475). Then one of the cytochrome P450 monooxygenases (apf7 or apf8) may oxidize this backbone to 2-oxooctanoic acid (PubMed:25058475). The aminotransferase apf4 is predicted to catalyze the exchange of the keto group with an amino group (PubMed:25058475). The next step would be the oxidation of 2-aminooctanoic acid by one of the cytochrome P450 monooxygenases (apf7 or apf8). The last step is the oxidation of 2-amino-8-hydroxyoctanoic acid to 2-aminooctanedioic acid is catalyzed by the FAD-dependent monooxygenase apf9 (PubMed:25058475).
 apf9 ELISA Kit
 apf9 Recombinant
 apf9 Antibody
 FFUJ_00005 ELISA Kit
 FFUJ_00005 Recombinant
 FFUJ_00005 Antibody
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FAD-linked oxidoreductase asqF

 FAD-linked oxidoreductase asqF ELISA Kit
 FAD-linked oxidoreductase asqF Recombinant
 FAD-linked oxidoreductase asqF Antibody
Also known as FAD-linked oxidoreductase asqF (4'-methoxyviridicatin/aspoquinolone biosynthesis cluster protein asqF) (Aspoquinolone biosynthesis protein F).
FAD-dependent dehydrogenase; 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 acid
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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).
 asqH ELISA Kit
 asqH Recombinant
 asqH Antibody
 AN9231 ELISA Kit
 AN9231 Recombinant
 AN9231 Antibody
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FAD-linked oxidoreductase azaG

 FAD-linked oxidoreductase azaG ELISA Kit
 FAD-linked oxidoreductase azaG Recombinant
 FAD-linked oxidoreductase azaG Antibody
Also known as FAD-linked oxidoreductase azaG (Azaphilone biosynthesis cluster protein azaG).
FAD-linked oxidoreductase; 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 polyketi
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de 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).
 azaG ELISA Kit
 azaG Recombinant
 azaG Antibody
 ASPNIDRAFT_189194 ELISA Kit
 ASPNIDRAFT_189194 Recombinant
 ASPNIDRAFT_189194 Antibody
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FAD-linked oxidoreductase azaL

 FAD-linked oxidoreductase azaL ELISA Kit
 FAD-linked oxidoreductase azaL Recombinant
 FAD-linked oxidoreductase azaL Antibody
Also known as FAD-linked oxidoreductase azaL (Azaphilone biosynthesis cluster protein azaL).
FAD-linked oxidoreductase; 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 polyketi
>>>
de 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).
 azaL ELISA Kit
 azaL Recombinant
 azaL Antibody
 ASPNIDRAFT_132654 ELISA Kit
 ASPNIDRAFT_132654 Recombinant
 ASPNIDRAFT_132654 Antibody
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FAD-linked oxidoreductase CHGG_01242-2

 FAD-linked oxidoreductase CHGG_01242-2 ELISA Kit
 FAD-linked oxidoreductase CHGG_01242-2 Recombinant
 FAD-linked oxidoreductase CHGG_01242-2 Antibody
Also known as FAD-linked oxidoreductase CHGG_01242-2 (Chaetoglobosin biosynthesis protein CHGG_01242-2).
FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of chaetoglobosin A which has a unique inhibitory activity against actin polymerization in mammalian cells (PubMed:23611317). The first step of the pathway is the synthesis of prochaetoglobosin I via condensat
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ion of one acetyl-CoA, 8 malonyl-CoA, and a L-tryptophan molecule by the PKS-NRPS hybrid synthetase CHGG_01239, followed by reduction of backbone double bond to install desired geometry by the enoyl reductase CHGG_01240 (PubMed:23611317). Further multiple oxidation steps performed by the cytochrome P450 monooxygenases CHGG_01242-1 and CHGG_01243, as well as by the FAD-linked oxidoreductase CHGG_01242-2, lead to the formation of chaetoglobosin A (PubMed:23611317). Depending on the order of action of these reductases, distinct intermediates can be identified (PubMed:23611317). Within the pathway, the cytochrome P450 monooxygenase CHGG_01242-1 catalyzes a stereospecific epoxidation on prochaetoglobosin I, cytoglobosin D, and chaetoglobosin J intermediates (PubMed:23611317). The FAD-linked oxidoreductase CHGG_01242-2 performs dehydrogenation of the C-20 hydroxyl groups in the 20-dihyrochaetoglobosin A and cytoglobosin D intermediates (PubMed:23611317). Finally, the cytochrome P450 monooxygenase CHGG_01243 can catalyze the stereospecific dihydroxylation of prochaetoglobosin I and prochaetoglobosin IV at C-19 and C-20, respectively (PubMed:23611317).
 CHGG_01242-2 ELISA Kit
 CHGG_01242-2 Recombinant
 CHGG_01242-2 Antibody
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FAD-linked oxidoreductase DDB_G0289697

 FAD-linked oxidoreductase DDB_G0289697 ELISA Kit
 FAD-linked oxidoreductase DDB_G0289697 Recombinant
 FAD-linked oxidoreductase DDB_G0289697 Antibody
 DDB_G0289697 ELISA Kit
 DDB_G0289697 Recombinant
 DDB_G0289697 Antibody
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FAD-linked oxidoreductase easE

 FAD-linked oxidoreductase easE ELISA Kit
 FAD-linked oxidoreductase easE Recombinant
 FAD-linked oxidoreductase easE Antibody
Also known as FAD-linked oxidoreductase easE (Ergot alkaloid synthesis protein E).
FAD binding oxidoreductase; part of the gene cluster that mediates the biosynthesis of fumiclavanine C, a fungal ergot alkaloid (PubMed:15933009, PubMed:23435153, PubMed:26972831). DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-
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dimethylallyl-L-tryptophan (PubMed:15870460). The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by EasD in the presence of NAD+, resulting in the formation of chanoclavine-I aldehyde (PubMed:20039019, PubMed:20526482, PubMed:21409592, PubMed:23435153). EasA reduces chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde that spontaneously dehydrates to form 6,8-dimethyl-6,7-didehydroergoline (PubMed:20526482). EasG then catalyzes the reduction of 6,8-dimethyl-6,7-didehydroergoline to form festuclavine (PubMed:20526482). Hydrolysis of festuclavine by easM then leads to the formation of fumigaclavine B which is in turn acetylated by easN to fumigaclavine A (PubMed:26972831). Finally, easL catalyzes the conversion of fumigaclavine A into fumigaclavine C by attaching a dimethylallyl moiety to C-2 of the indole nucleus (PubMed:19672909).
 easE ELISA Kit
 easE Recombinant
 easE Antibody
 AFUA_2G18050 ELISA Kit
 AFUA_2G18050 Recombinant
 AFUA_2G18050 Antibody
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FAD-linked oxidoreductase hmp9

 FAD-linked oxidoreductase hmp9 ELISA Kit
 FAD-linked oxidoreductase hmp9 Recombinant
 FAD-linked oxidoreductase hmp9 Antibody
Also known as FAD-linked oxidoreductase hmp9 (Hypothemycin biosynthesis cluster protein hpm9).
FAD-linked oxidoreductase; 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 is performed
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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).
 hpm9 ELISA Kit
 hpm9 Recombinant
 hpm9 Antibody
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FAD-linked oxidoreductase patO

 FAD-linked oxidoreductase patO ELISA Kit
 FAD-linked oxidoreductase patO Recombinant
 FAD-linked oxidoreductase patO Antibody
Also known as FAD-linked oxidoreductase patO (Patulin synthesis protein O).
FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (PubMed:19383676, PubMed:24334092). The pathway begins with the synthesis of 6-methylsali
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cylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units (PubMed:19383676). PatG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (PubMed:24334092). The cytochrome P450 monooxygenase patH then converts m-cresol to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI (PubMed:19383676). The conversion of gentisyl alcohol to two-ring compound neopatulin remains a matter of speculation, but it involves at least two intermediates, isoepoxydon and phyllostin (PubMed:19383676). PatN catalyzes the transformation of isoepoxydon into phyllostin (PubMed:19383676). The last part of the biosynthetic pathway involves the conversion of neopatulin to ascladiol followed by the transformation of the latter into patulin (PubMed:19383676).
 patO ELISA Kit
 patO Recombinant
 patO Antibody
 ACLA_093700 ELISA Kit
 ACLA_093700 Recombinant
 ACLA_093700 Antibody
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