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Oxidoreductase

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Monooxygenase; part of the gene cluster that mediates the biosynthesis of aflatoxins, a group of polyketide-derived furanocoumarins, and part of the most toxic and carcinogenic compounds among the known mycotoxins .

Below are the list of possible 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.
 

Oxidoreductase AflX

 Oxidoreductase AflX ELISA Kit
 Oxidoreductase AflX Recombinant
 Oxidoreductase AflX Antibody
Also known as Oxidoreductase AflX (Aflatoxin biosynthesis protein X).
Monooxygenase; part of the gene cluster that mediates the biosynthesis of aflatoxins, a group of polyketide-derived furanocoumarins, and part of the most toxic and carcinogenic compounds among the known mycotoxins (PubMed:15006741). The four major aflatoxins produced by A.parasiticus are aflatoxin B1 (AFB1), aflatoxin B2 (AFB
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2), aflatoxin G1 (AFG1) and aflatoxin G2 (AFG2) (PubMed:15006741). The first step of the pathway is the conversion of acetate to norsolorinic acid (NOR) and requires the fatty acid synthase subunits aflA and aflB, as well as the PKS aflC (PubMed:15006741). AflC combines a hexanoyl starter unit and 7 malonyl-CoA extender units to synthesize the precursor NOR (PubMed:18403714). The hexanoyl starter unit is provided to the acyl-carrier protein (ACP) domain by the fungal fatty acid synthase aflA/aflB (PubMed:16256699). The second step is the conversion of NOR to averantin (AVN) and requires the norsolorinic acid ketoreductase aflD, which catalyzes the dehydration of norsolorinic acid to form (1'S)-averantin (PubMed:10584035). The norsolorinic acid reductases aflE and aflF may also play a role in the conversion of NOR to AVN (PubMed:15006741). The cytochrome P450 monooxygenase aflG then catalyzes the hydroxylation of AVN to 5'hydroxyaverantin (HAVN) (PubMed:8368836). The next step is performed by the 5'-hydroxyaverantin dehydrogenase aflH that transforms HAVN to 5'-oxoaverantin (OAVN) which is further converted to averufin (AVF) by aflK that plays a dual role in the pathway, as a 5'-oxoaverantin cyclase that mediates conversion of 5'-oxoaverantin, as well as a versicolorin B synthase in a later step in the pathway (PubMed:15006741, PubMed:11055914, PubMed:15932995). The averufin oxidase aflI catalyzes the conversion of AVF to versiconal hemiacetal acetate (VHA) (PubMed:15006741). VHA is then the substrate for the versiconal hemiacetal acetate esterase aflJ to yield versiconal (VAL) (PubMed:15006741). Versicolorin B synthase aflK then converts VAL to versicolorin B (VERB) by closing the bisfuran ring of aflatoxin which is required for DNA-binding, thus giving to aflatoxin its activity as a mutagen (PubMed:15006741, PubMed:8368837, PubMed:15932995). Then, the activity of the versicolorin B desaturase aflL leads to versicolorin A (VERA) (PubMed:15006741, PubMed:8368837). A branch point starts from VERB since it can also be converted to dihydrodemethylsterigmatocystin (DMDHST), probably also by aflL, VERA being a precursor for aflatoxins B1 and G1, and DMDHST for aflatoxins B2 and G2 (PubMed:15006741). Next, the versicolorin reductase aflM and the cytochrome P450 monooxygenase aflN are involved in conversion of VERA to demethylsterigmatocystin (DMST) (PubMed:15006741, PubMed:1339261, PubMed:15771506). AflX and aflY seem also involved in this step, through probable aflX-mediated epoxide ring-opening step following versicolorin A oxidation and aflY-mediated Baeyer-Villiger oxidation required for the formation of the xanthone ring (PubMed:16332900, PubMed:16461654). The methyltransferase aflO then leads to the modification of DMST to sterigmatocystin (ST), and of DMDHST to dihydrosterigmatocystin (DHST) (PubMed:10543813). Both ST and DHST are then substrates of the O-methyltransferase aflP to yield O-methylsterigmatocystin (OMST) and dihydro-O-methylsterigmatocystin (DHOMST), respectively (PubMed:8434913). Finally OMST is converted to aflatoxins B1 and G1, and DHOMST to aflatoxins B2 and G2, via the action of several enzymes including O-methylsterigmatocystin oxidoreductase aflQ, the cytodhrome P450 monooxygenase aflU, but also the NADH-dependent flavin oxidoreductase nadA which is specifically required for the synthesis of AFG1 (PubMed:15006741, PubMed:11996570, PubMed:15528514, PubMed:18486503).
 aflX ELISA Kit
 aflX Recombinant
 aflX Antibody
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Oxidoreductase AflY

 Oxidoreductase AflY ELISA Kit
 Oxidoreductase AflY Recombinant
 Oxidoreductase AflY Antibody
Also known as Oxidoreductase AflY (Aflatoxin biosynthesis protein Y).
Oxidoreductase; part of the gene cluster that mediates the biosynthesis of aflatoxins, a group of polyketide-derived furanocoumarins, and part of the most toxic and carcinogenic compounds among the known mycotoxins (PubMed:15094053, PubMed:15006741). The four major aflatoxins produced by A.parasiticus are aflatoxin B1 (AFB1),
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aflatoxin B2 (AFB2), aflatoxin G1 (AFG1) and aflatoxin G2 (AFG2) (PubMed:15006741). The first step of the pathway is the conversion of acetate to norsolorinic acid (NOR) and requires the fatty acid synthase subunits aflA and aflB, as well as the PKS aflC (PubMed:15006741). AflC combines a hexanoyl starter unit and 7 malonyl-CoA extender units to synthesize the precursor NOR (PubMed:18403714). The hexanoyl starter unit is provided to the acyl-carrier protein (ACP) domain by the fungal fatty acid synthase aflA/aflB (PubMed:16256699). The second step is the conversion of NOR to averantin (AVN) and requires the norsolorinic acid ketoreductase aflD, which catalyzes the dehydration of norsolorinic acid to form (1'S)-averantin (PubMed:10584035). The norsolorinic acid reductases aflE and aflF may also play a role in the conversion of NOR to AVN (PubMed:15006741). The cytochrome P450 monooxygenase aflG then catalyzes the hydroxylation of AVN to 5'hydroxyaverantin (HAVN) (PubMed:8368836). The next step is performed by the 5'-hydroxyaverantin dehydrogenase aflH that transforms HAVN to 5'-oxoaverantin (OAVN) which is further converted to averufin (AVF) by aflK that plays a dual role in the pathway, as a 5'-oxoaverantin cyclase that mediates conversion of 5'-oxoaverantin, as well as a versicolorin B synthase in a later step in the pathway (PubMed:15006741, PubMed:11055914, PubMed:15932995). The averufin oxidase aflI catalyzes the conversion of AVF to versiconal hemiacetal acetate (VHA) (PubMed:15006741). VHA is then the substrate for the versiconal hemiacetal acetate esterase aflJ to yield versiconal (VAL) (PubMed:15006741). Versicolorin B synthase aflK then converts VAL to versicolorin B (VERB) by closing the bisfuran ring of aflatoxin which is required for DNA-binding, thus giving to aflatoxin its activity as a mutagen (PubMed:15006741, PubMed:8368837, PubMed:15932995). Then, the activity of the versicolorin B desaturase aflL leads to versicolorin A (VERA) (PubMed:15006741, PubMed:8368837). A branch point starts from VERB since it can also be converted to dihydrodemethylsterigmatocystin (DMDHST), probably also by aflL, VERA being a precursor for aflatoxins B1 and G1, and DMDHST for aflatoxins B2 and G2 (PubMed:15006741). Next, the versicolorin reductase aflM and the cytochrome P450 monooxygenase aflN are involved in conversion of VERA to demethylsterigmatocystin (DMST) (PubMed:15006741, PubMed:1339261, PubMed:15771506). AflX and aflY seem also involved in this step, through probable aflX-mediated epoxide ring-opening step following versicolorin A oxidation and aflY-mediated Baeyer-Villiger oxidation required for the formation of the xanthone ring (PubMed:16332900, PubMed:16461654). The methyltransferase aflO then leads to the modification of DMST to sterigmatocystin (ST), and of DMDHST to dihydrosterigmatocystin (DHST) (PubMed:10543813). Both ST and DHST are then substrates of the O-methyltransferase aflP to yield O-methylsterigmatocystin (OMST) and dihydro-O-methylsterigmatocystin (DHOMST), respectively (PubMed:8434913). Finally OMST is converted to aflatoxins B1 and G1, and DHOMST to aflatoxins B2 and G2, via the action of several enzymes including O-methylsterigmatocystin oxidoreductase aflQ, the cytodhrome P450 monooxygenase aflU, but also the NADH-dependent flavin oxidoreductase nadA which is specifically required for the synthesis of AFG1 (PubMed:15006741, PubMed:11996570, PubMed:15528514, PubMed:18486503).
 aflY ELISA Kit
 aflY Recombinant
 aflY Antibody
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Oxidoreductase andH

 Oxidoreductase andH ELISA Kit
 Oxidoreductase andH Recombinant
 Oxidoreductase andH Antibody
Also known as Oxidoreductase andH (Anditomin synthesis protein H).
Oxidoreductase; 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 compound 5,7-dihydroxy-4,6
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-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).
 andH ELISA Kit
 andH Recombinant
 andH Antibody
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Oxidoreductase HTATIP2

 Oxidoreductase HTATIP2 ELISA Kit
 Oxidoreductase HTATIP2 Recombinant
 Oxidoreductase HTATIP2 Antibody
Oxidoreductase required for tumor suppression. NAPDH-bound form inhibits nuclear import by competing with nuclear import substrates for binding to a subset of nuclear transport receptors. May act as a redox sensor linked to transcription through regulation of nuclear import ().
 HTATIP2 ELISA Kit
 HTATIP2 Recombinant
 HTATIP2 Antibody
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Oxidoreductase NdmD

 Oxidoreductase NdmD ELISA Kit
 Oxidoreductase NdmD Recombinant
 Oxidoreductase NdmD Antibody
Involved in the caffeine degradation, which is the essential first step for assimilating the carbon and nitrogen in caffeine. Catalyzes the oxidation of NADH and transfers electrons to NdmA and NdmB, which catalyze the N-demethylation reactions.
 ndmD ELISA Kit
 ndmD Recombinant
 ndmD Antibody
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Oxidoreductase PigB

 Oxidoreductase PigB ELISA Kit
 Oxidoreductase PigB Recombinant
 Oxidoreductase PigB Antibody
Involved in the biosynthesis of 2-methyl-3-n-amyl-pyrrole (MAP), one of the terminal products involved in the biosynthesis of the red antibiotic prodigiosin (Pig). Catalyzes the oxidation of dihydro form of MAP (H2MAP) to yield MAP.
 pigB ELISA Kit
 pigB Recombinant
 pigB Antibody
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Oxidoreductase sirO

 Oxidoreductase sirO ELISA Kit
 Oxidoreductase sirO Recombinant
 Oxidoreductase sirO Antibody
Also known as Oxidoreductase sirO (Sirodesmin biosynthesis protein O).
Oxidoreductase; part of the gene cluster that mediates the biosynthesis of sirodesmin PL, an epipolythiodioxopiperazine (ETP) characterized by a disulfide bridged cyclic dipeptide and that acts as a phytotoxin which is involved in the blackleg didease of canola (PubMed:15387811, PubMed:18272357, PubMed:19762440). SirD cataly
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zes the O-prenylation of L-tyrosine (L-Tyr) in the presence of dimethylallyl diphosphate (DMAPP) to yield 4-O-dimethylallyl-L-Tyr, and therefore represents probably the first pathway-specific enzyme in the biosynthesis of sirodesmin PL (PubMed:19762440, PubMed:21038099, PubMed:24083562). 4-O-dimethylallyl-L-Tyr, then undergoes condensation with L-Ser in a reaction catalyzed by the non-ribosomal peptide synthase sirP to form the diketopiperazine (DKP) backbone (PubMed:18272357). Further bishydroxylation of the DKP performed by the cytochrome P450 monooxygenase sirC leads to the production of the intermediate phomamide (PubMed:27390873). This step is essential to form the reactive thiol group required for toxicity of sirodesmin PL (PubMed:27390873). The next steps of sirodesmin biosynthesis are not well understood yet, but some predictions could be made from intermediate compounds identification (PubMed:18272357). Phomamide is converted into phomalizarine via oxidation, probably by sirT (PubMed:18272357). Further oxidation, methylation (by sirM or sirN) and reduction steps convert phomalizarine to deacetyl sirodesmin (PubMed:18272357). Finally, acetyltransferase sirH probably acetylates deacetyl sirodesmin to produce sirodesmin PL (PubMed:18272357).
 sirO ELISA Kit
 sirO Recombinant
 sirO Antibody
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Oxidoreductase tpcJ

 Oxidoreductase tpcJ ELISA Kit
 Oxidoreductase tpcJ Recombinant
 Oxidoreductase tpcJ Antibody
Also known as Oxidoreductase tpcJ (Trypacidin synthesis protein J).
Oxidoreductase; part of the gene cluster that mediates the biosynthesis of trypacidin, a mycotoxin with antiprotozoal activity and that plays a role in the infection process (PubMed:26278536, PubMed:26242966). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) tpcC (PubMed:26242966). The atrochrysone carboxyl ACP thioesterase tpcB then breaks the thioester bond and releases the atrochrysone carboxylic acid from tpcC (PubMed:26242966). The decarboxylase tpcK converts atrochrysone
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carboxylic acid to atrochrysone which is further reduced into emodin anthrone (PubMed:26242966). The next step is performed by the emodin anthrone oxygenase tpcL that catalyzes the oxidation of emodinanthrone to emodin (PubMed:26242966). Emodin O-methyltransferase encoded by tpcA catalyzes methylation of the 8-hydroxy group of emodin to form questin (PubMed:26242966). Ring cleavage of questin by questin oxidase tpcI leads to desmethylsulochrin via several intermediates including questin epoxide (). Another methylation step catalyzed by tpcM leads to the formation of sulochrin which is further converted to monomethylsulfochrin by tpcH. Finally, the tpcJ catalyzes the conversion of monomethylsulfochrin to trypacidin (PubMed:26242966). Trypacidin is toxic for human pulmonary and bronchial epithelial cells by initiating the intracellular formation of nitric oxide (NO) and hydrogen peroxide (H2O2), thus triggering host necrotic cell death (PubMed:22319557). The trypacidin pathway is also able to produce endocrocin via a distinct route from the endocrocin Enc pathway (PubMed:26242966).
 tpcJ ELISA Kit
 tpcJ Recombinant
 tpcJ Antibody
 tynJ ELISA Kit
 tynJ Recombinant
 tynJ Antibody
 AFUA_4G14490 ELISA Kit
 AFUA_4G14490 Recombinant
 AFUA_4G14490 Antibody
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Oxidoreductase UcpA

 Oxidoreductase UcpA ELISA Kit
 Oxidoreductase UcpA Recombinant
 Oxidoreductase UcpA Antibody
 ucpA ELISA Kit
 ucpA Recombinant
 ucpA Antibody
 STY2682 ELISA Kit
 STY2682 Recombinant
 STY2682 Antibody
 t0413 ELISA Kit
 t0413 Recombinant
 t0413 Antibody
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Oxidoreductase vrtI

 Oxidoreductase vrtI ELISA Kit
 Oxidoreductase vrtI Recombinant
 Oxidoreductase vrtI Antibody
Also known as Oxidoreductase vrtI (Viridicatumtoxin synthesis protein I).
Oxidoreductase; 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 polyketide synthase vrtA (PubMed
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: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).
 vrtI ELISA Kit
 vrtI Recombinant
 vrtI Antibody
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Oxidoreductase YdhF

 Oxidoreductase YdhF ELISA Kit
 Oxidoreductase YdhF Recombinant
 Oxidoreductase YdhF Antibody
May function as oxidoreductase.
 ydhF ELISA Kit
 ydhF Recombinant
 ydhF Antibody
 b1647 ELISA Kit
 b1647 Recombinant
 b1647 Antibody
 JW1639 ELISA Kit
 JW1639 Recombinant
 JW1639 Antibody
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