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Non-reducing polyketide synthase

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Non-reducing polyketide synthase (NRPKS); part of the gene cluster that mediates the biosynthesis of aflavarin, a bicoumarin that exhibits anti-insectan activity against the fungivorous beetle C.hemipterus (Ref.2, PubMed:26209694). Catalyzes the formation of the aromatic polyketide from acetyl coenzyme A and seven malonyl coenzyme A molecules .

Below are the list of possible Non-reducing polyketide synthase 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.
 

Non-reducing polyketide synthase afvB

 Non-reducing polyketide synthase afvB ELISA Kit
 Non-reducing polyketide synthase afvB Recombinant
 Non-reducing polyketide synthase afvB Antibody
Also known as Non-reducing polyketide synthase afvB (NRPKS) (Aflavarin synthesis protein B).
Non-reducing polyketide synthase (NRPKS); part of the gene cluster that mediates the biosynthesis of aflavarin, a bicoumarin that exhibits anti-insectan activity against the fungivorous beetle C.hemipterus (Ref. 2, PubMed:26209694). Catalyzes the formation of the aromatic polyketide from acetyl coenzyme
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A and seven malonyl coenzyme A molecules (PubMed:26209694).
 afvB ELISA Kit
 afvB Recombinant
 afvB Antibody
 AFLA_108550 ELISA Kit
 AFLA_108550 Recombinant
 AFLA_108550 Antibody
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Non-reducing polyketide synthase andM

 Non-reducing polyketide synthase andM ELISA Kit
 Non-reducing polyketide synthase andM Recombinant
 Non-reducing polyketide synthase andM Antibody
Also known as Non-reducing polyketide synthase andM (Anditomin synthesis protein M).
Non-reducing polyketide synthase; 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
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phthalide 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).
 andM ELISA Kit
 andM Recombinant
 andM Antibody
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Non-reducing polyketide synthase aptA

 Non-reducing polyketide synthase aptA ELISA Kit
 Non-reducing polyketide synthase aptA Recombinant
 Non-reducing polyketide synthase aptA Antibody
Also known as Non-reducing polyketide synthase aptA (NRPKS) (Asperthecin synthesis protein A).
Non-reducing polyketide synthase (NRPKS); part of the gene cluster that mediates the biosynthesis of asperthecin, an anthraquinone pigment (PubMed:18978088, PubMed:21866960). Catalyzes the formation of the aromatic polyketide from acetyl coenzyme A and seven malonyl coenzyme A molecules (PubMed:189780
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88, PubMed:21866960). Through its product template (PT) domain, catalyzes the cyclization of the polyketide backbone via C6-C11 aldolcondensation (PubMed:20479000). Polyketide is subsequently hydrolyzed from the NRPKS by the action of the hydrolase aptB into endocrocin-9-anthrone (PubMed:18978088). Endocrocin-9-anthrone is then oxidized into endocrocin by 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).
 aptA ELISA Kit
 aptA Recombinant
 aptA Antibody
 AN6000.2 ELISA Kit
 AN6000.2 Recombinant
 AN6000.2 Antibody
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Non-reducing polyketide synthase ausA

 Non-reducing polyketide synthase ausA ELISA Kit
 Non-reducing polyketide synthase ausA Recombinant
 Non-reducing polyketide synthase ausA Antibody
Also known as Non-reducing polyketide synthase ausA (Austinol synthesis protein A) (Methylorcinaldehyde synthase ausA).
Non-reducing polyketide synthase; 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 au
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sA (PubMed:22329759). 3,5-dimethylorsellinic acid 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).
 ausA ELISA Kit
 ausA Recombinant
 ausA Antibody
 AN8383 ELISA Kit
 AN8383 Recombinant
 AN8383 Antibody
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Non-reducing polyketide synthase azaA

 Non-reducing polyketide synthase azaA ELISA Kit
 Non-reducing polyketide synthase azaA Recombinant
 Non-reducing polyketide synthase azaA Antibody
Also known as Non-reducing polyketide synthase azaA (NR-PKS azaA) (Azaphilone biosynthesis cluster protein azaA).
Non-reducing polyketide synthase; 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 ste
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p, the non-reducing polyketide 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).
 azaA ELISA Kit
 azaA Recombinant
 azaA Antibody
 ASPNIDRAFT_56946 ELISA Kit
 ASPNIDRAFT_56946 Recombinant
 ASPNIDRAFT_56946 Antibody
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Non-reducing polyketide synthase cla3

 Non-reducing polyketide synthase cla3 ELISA Kit
 Non-reducing polyketide synthase cla3 Recombinant
 Non-reducing polyketide synthase cla3 Antibody
Also known as Non-reducing polyketide synthase cla3 (Cladosporin bioynthesis cluster protein 3).
Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of cladosporin, a tricyclic octaketide that acts as an antimalarial agent though inhibition of the Plasmodium falciparum lysyl-tRNA synthetase (PubMed:26783060). The highly reducing polyketide synthase cla2
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is responsible for biosynthesis up to the pentaketide stage, including of the tetrahydropyran (THP) ring, whereas the three subsequent ketide extensions with no reduction are catalyzed by the non-reducing polyketide synthase cla3 (PubMed:26783060).
 cla3 ELISA Kit
 cla3 Recombinant
 cla3 Antibody
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Non-reducing polyketide synthase gsfA

 Non-reducing polyketide synthase gsfA ELISA Kit
 Non-reducing polyketide synthase gsfA Recombinant
 Non-reducing polyketide synthase gsfA Antibody
Also known as Non-reducing polyketide synthase gsfA (Griseofulvin synthesis protein A) (Norlichexanthone synthase).
Norlichexanthone synthase; part of the gene cluster that mediates the biosynthesis of griseofulvin, an important antifungal drug that has been in use for a long time for treating dermatophyte infections (PubMed:20534346, PubMed:23978092). The first step of the pathway is the forma
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tion of the heptaketide backbone by gsfA which is initiated by priming with acetyl-CoA, followed by sequential condensations of 6 malonyl-CoA units (PubMed:20534346). O-methylation at 3-OH by gsfB leads to griseophenone D which is further methylated at 9-OH by gsfC to yield griseophenone C (PubMed:23978092). Griseophenone C is then substrate of halogenase gsfI which is responsible for the regio-specific chlorination at the C13 position to form griseophenone B (PubMed:23978092). The cytochrome P450 gsfF catalyzes the coupling of orcinol and phloroglucinol rings in griseophenone B to form desmethyl-dehydrogriseofulvin A which is further methylated at 5-OH by gsfD to yield dehydrogriseofulvin (PubMed:23978092). Finally, gsfE performs stereospecific reduction of enone 18 of dehydrogriseofulvin to afford the final product griseofulvin (PubMed:23978092).
 gsfA ELISA Kit
 gsfA Recombinant
 gsfA Antibody
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Non-reducing polyketide synthase hmp3

 Non-reducing polyketide synthase hmp3 ELISA Kit
 Non-reducing polyketide synthase hmp3 Recombinant
 Non-reducing polyketide synthase hmp3 Antibody
Also known as Non-reducing polyketide synthase hmp3 (NR-PKS hmp3) (Hypothemycin biosynthesis cluster protein hpm3).
Non-reducing polyketide synthase; 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).
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The first step is 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).
 hpm3 ELISA Kit
 hpm3 Recombinant
 hpm3 Antibody
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Non-reducing polyketide synthase mapC

 Non-reducing polyketide synthase mapC ELISA Kit
 Non-reducing polyketide synthase mapC Recombinant
 Non-reducing polyketide synthase mapC Antibody
Also known as Non-reducing polyketide synthase mapC (Mycophenolic acid synthesis protein C).
Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of mycophenolic acid (MPA), the first natural antibiotic isolated in the world (PubMed:21398490, PubMed:22544261, PubMed:25630520). The first step of the pathway is the synthesis of 5-methylorsellinic acid (5MOA) b
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y the polyketide synthase mpaC (PubMed:21398490). 5MOA is then converted to the phthalide compound 5,7-dihydroxy-4,6-dimethylphthalide (DHDMP) by mpaDE (PubMed:22544261). MpaDE first catalyzes hydroxylation of 5-MOA to 4,6-dihydroxy-2-(hydroxymethyl)-3-methylbenzoic acid (DHMB) (PubMed:22544261). MpaDE then acts as a lactone synthase that catalyzes the ring closure, converting DHMB to DHMP (PubMed:22544261). The next step is the prenylation of DHMP by the prenyltransferase mpaA to yield farnesyl-DHDMP (PubMed:25630520). Farnesyl-DHDMP might be a substrate of mpaH for transformation into demethylmycophenolic acid (DMMPA) (PubMed:25630520). Finally, the O-methyltransferase mpaG catalyzes the methylation DMMPA to form MPA (PubMed:25630520).
 mpaC ELISA Kit
 mpaC Recombinant
 mpaC Antibody
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Non-reducing polyketide synthase nscA

 Non-reducing polyketide synthase nscA ELISA Kit
 Non-reducing polyketide synthase nscA Recombinant
 Non-reducing polyketide synthase nscA Antibody
Also known as Non-reducing polyketide synthase nscA (Conidial yellow pigment biosynthesis polyketide synthase nscA) (Neosartoricin B biosynthesis protein A).
Non-reducing polyketide synthase; 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 immu
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nosuppressive agent (PubMed:23758576, PubMed:23368997). The non-reducing polyketide synthase 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 ().
 nscA ELISA Kit
 nscA Recombinant
 nscA Antibody
 MCYG_03598 ELISA Kit
 MCYG_03598 Recombinant
 MCYG_03598 Antibody
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Non-reducing polyketide synthase pks27

 Non-reducing polyketide synthase pks27 ELISA Kit
 Non-reducing polyketide synthase pks27 Recombinant
 Non-reducing polyketide synthase pks27 Antibody
Also known as Non-reducing polyketide synthase pks27 (NRPKS) (Asparasone A synthesis protein pks27) (Cluster 27 polyketide synthase).
Non-reducing polyketide synthase (NRPKS); part of the gene cluster 27 that mediates the biosynthesis of asparasone A, a sclerotium-specific anthraquinone pigment important for sclerotial survival (PubMed:24405210, PubMed:24412484). Catalyzes the formation of the
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aromatic polyketide from acetyl coenzyme A and seven malonyl coenzyme A molecules (PubMed:24405210). Through its product template (PT) domain, catalyzes the cyclization of polyketide backbone via C6-C11 aldolcondensation ().
 pks27 ELISA Kit
 pks27 Recombinant
 pks27 Antibody
 AFLA_082150 ELISA Kit
 AFLA_082150 Recombinant
 AFLA_082150 Antibody
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Non-reducing polyketide synthase pyr2

 Non-reducing polyketide synthase pyr2 ELISA Kit
 Non-reducing polyketide synthase pyr2 Recombinant
 Non-reducing polyketide synthase pyr2 Antibody
Also known as Non-reducing polyketide synthase pyr2 (Pyripyropene synthesis protein 2).
Non-reducing polyketide synthase; 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-Co
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A ligase pyr1 (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).
 pyr2 ELISA Kit
 pyr2 Recombinant
 pyr2 Antibody
 AFUA_6G13930 ELISA Kit
 AFUA_6G13930 Recombinant
 AFUA_6G13930 Antibody
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Non-reducing polyketide synthase rdc1

 Non-reducing polyketide synthase rdc1 ELISA Kit
 Non-reducing polyketide synthase rdc1 Recombinant
 Non-reducing polyketide synthase rdc1 Antibody
Also known as Non-reducing polyketide synthase rdc1 (NR-PKS rdc1) (Radicicol biosynthesis cluster protein rdc1).
Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of radicicol, a resorcylic acid lactone (RAL) that irreversibly inhibits the HSP90 molecular chaperone, an important target for cancer chemotherapy (PubMed:18567690). The cluster encodes only tw
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o apparent post-PKS enzymes, a cytochrome P450 monooxygenase (rdc4) and a non-heme halogenase (rdc2) that could introduce the epoxide and the chlorine, respectively (PubMed:18567690). If this cluster includes all the genes required for radicicol biosynthesis, the remaining structural features of radicicol are presumably generated by the PKSs rdc1 and rdc5 (PubMed:18567690). The C-2' ketone could arise if the R-PKS rdc5 and NR-PKS rdc1 each carry out four iterations, in contrast to the five iteration-three iteration split for the hypothemycin PKSs (PubMed:18567690). The origin of the cis 5',6' double bond is not known (PubMed:18567690). The radicicol R-PKS rdc5 ER domain may catalyze either double bond isomerization or reduction in the third iteration (PubMed:18567690).
 rdc1 ELISA Kit
 rdc1 Recombinant
 rdc1 Antibody
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Non-reducing polyketide synthase terA

 Non-reducing polyketide synthase terA ELISA Kit
 Non-reducing polyketide synthase terA Recombinant
 Non-reducing polyketide synthase terA Antibody
Also known as Non-reducing polyketide synthase terA (Terrein biosynthesis cluster protein terA).
Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of terrein, a fungal metabolite with ecological, antimicrobial, antiproliferative, and antioxidative activities (PubMed:24816227, PubMed:26173180). The first step in the pathway is performed by the polyketide s
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ynthase terA that produces 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).
 terA ELISA Kit
 terA Recombinant
 terA Antibody
 ATEG_00145 ELISA Kit
 ATEG_00145 Recombinant
 ATEG_00145 Antibody
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Non-reducing polyketide synthase trt4

 Non-reducing polyketide synthase trt4 ELISA Kit
 Non-reducing polyketide synthase trt4 Recombinant
 Non-reducing polyketide synthase trt4 Antibody
Also known as Non-reducing polyketide synthase trt4 (Terretonin synthesis protein 4).
Non-reducing polyketide synthase; 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 sy
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nthase trt4 (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).
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 ATEG_10080 ELISA Kit
 ATEG_10080 Recombinant
 ATEG_10080 Antibody
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Non-reducing polyketide synthase vrtA

 Non-reducing polyketide synthase vrtA ELISA Kit
 Non-reducing polyketide synthase vrtA Recombinant
 Non-reducing polyketide synthase vrtA Antibody
Also known as Non-reducing polyketide synthase vrtA (Viridicatumtoxin synthesis protein A).
Non-reducing polyketide synthase; 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
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the polyketide 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).
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 vrtA Recombinant
 vrtA Antibody
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Non-reducing polyketide synthase yanA

 Non-reducing polyketide synthase yanA ELISA Kit
 Non-reducing polyketide synthase yanA Recombinant
 Non-reducing polyketide synthase yanA Antibody
Also known as Non-reducing polyketide synthase yanA (Yanuthone D synthesis protein A).
Non-reducing polyketide synthase; 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 synthase 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
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to toluquinol (PubMed:24684908). Epoxidation of toluquinol is then performed by the short chain dehydrogenase yanD, with the help of yanE, and a further prenylation 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).
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 yanA Recombinant
 yanA Antibody
 pks48 ELISA Kit
 pks48 Recombinant
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 ASPNIDRAFT_44965 ELISA Kit
 ASPNIDRAFT_44965 Recombinant
 ASPNIDRAFT_44965 Antibody
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