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N-methyltransferase

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N-methyltransferase; part of the gene cluster that mediates the biosynthesis of the dimeric diketopiperazine alkaloid ditryptophenaline .

Below are the list of possible N-methyltransferase 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.
 

N-methyltransferase dtpB

 N-methyltransferase dtpB ELISA Kit
 N-methyltransferase dtpB Recombinant
 N-methyltransferase dtpB Antibody
Also known as N-methyltransferase dtpB (Ditryptophenaline biosynthesis protein B).
N-methyltransferase; part of the gene cluster that mediates the biosynthesis of the dimeric diketopiperazine alkaloid ditryptophenaline (PubMed:24677498). The nonribosomal peptide synthase dtpA accepts L-tryptophan and L-phenylalanine as its substrates and forms the phenylalanyl-tryptophanyl cyclic dipeptide prod
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uct cyclophenylalanyltryptophenyl (PubMed:24677498). The N-methyltransferase dtpB is responsible for the N-methylation of cyclophenylalanyltryptophenyl to yield cyclo-N-methylphenylalanyltryptophenyl (PubMed:24677498). The cytochrome P450 monooxygenase is responsible not only for pyrroloindole ring formation but also for concurrent dimerization of N-methylphenylalanyltryptophanyl diketopiperazine monomers into a homodimeric product (PubMed:24677498).
 dtpB ELISA Kit
 dtpB Recombinant
 dtpB Antibody
 AFLA_005450 ELISA Kit
 AFLA_005450 Recombinant
 AFLA_005450 Antibody
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N-methyltransferase gliN

 N-methyltransferase gliN ELISA Kit
 N-methyltransferase gliN Recombinant
 N-methyltransferase gliN Antibody
Also known as N-methyltransferase gliN (Gliotoxin biosynthesis protein N).
N-methyltransferase; part of the gene cluster that mediates the biosynthesis of gliotoxin, a member of the epipolythiodioxopiperazine (ETP) class of toxins characterized by a disulfide bridged cyclic dipeptide (PubMed:15979823, PubMed:21612254). The first step in gliotoxin biosynthesis is the condensation of serine and p
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henylalanine to form the cyclo-L-phenylalanyl-L-serine diketopiperazine (DKP) by the NRPS gliP (PubMed:17154540, PubMed:21612254). GliP is also able to produce the DKP cyclo-L-tryptophanyl-L-serine, suggesting that the substrate specificity of the first adenylation (A) domain in gliP is sufficiently relaxed to accommodate both L-Phe and L-Trp (PubMed:23434416). The cytochrome P450 monooxygenase gliC has been shown to catalyze the subsequent hydroxylation of the alpha-carbon of L-Phe in cyclo-L-phenylalanyl-L-serine whereas the second cytochrome P450 enzyme, gliF, is presumably involved in the modification of the DKP side chain (PubMed:24039048, PubMed:23434416). The glutathione S-transferase (GST) gliG then forms a bis-glutathionylated biosynthetic intermediate which is responsible for the sulfurization of gliotoxin (PubMed:21513890, PubMed:21749092). This bis-glutathionylated intermediate is subsequently processed by the gamma-glutamyl cyclotransferase gliK to remove both gamma-glutamyl moieties (PubMed:22903976, PubMed:24039048). Subsequent processing via gliI yields a biosynthetic intermediate, which is N-methylated via the N-methyltransferase gliN, before the gliotoxin oxidoreductase gliT-mediated disulfide bridge closure (PubMed:20548963, PubMed:22936680, PubMed:24039048, PubMed:25062268). GliN-mediated amide methylation confers stability to ETP, damping the spontaneous formation of tri- and tetrasulfides (PubMed:25062268). Intracellular dithiol gliotoxin oxidized by gliT is subsequently effluxed by gliA (PubMed:26150413). Gliotoxin contributes to pathogenesis during invasive aspergillosis (PubMed:17601876, PubMed:18199036). In macrophages and neutrophils, gliotoxin showed inhibition of various different cell functions including cytokine production, antigen presentation, phagocytosis, and production of reactive oxygen species (PubMed:17601876).
 gliN ELISA Kit
 gliN Recombinant
 gliN Antibody
 AFUA_6G09720 ELISA Kit
 AFUA_6G09720 Recombinant
 AFUA_6G09720 Antibody
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N-methyltransferase sirN

 N-methyltransferase sirN ELISA Kit
 N-methyltransferase sirN Recombinant
 N-methyltransferase sirN Antibody
Also known as N-methyltransferase sirN (Sirodesmin biosynthesis protein N).
N-methyltransferase; 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). S
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irD catalyzes 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).
 sirN ELISA Kit
 sirN Recombinant
 sirN Antibody
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N-methyltransferase tcpN

 N-methyltransferase tcpN ELISA Kit
 N-methyltransferase tcpN Recombinant
 N-methyltransferase tcpN Antibody
Also known as N-methyltransferase tcpN (Thioclapurine biosynthesis protein N).
N-methyltransferase; part of the gene cluster that mediates the biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) lacking the reactive thiol group important for toxicity (PubMed:27390873). Firstly, L-tyrosine is prenylated by tcpD, before undergoing condensation with L-glycine in a reaction catal
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yzed by the NRPS tcpP leading to the diketopiperazine (DKP) backbone (PubMed:27390873). Afterwards the alpha-carbon of tyrosine is oxidized by the cytochrome P450 tcpC to form a hydroxyl group (PubMed:27390873). However, in contrast other ETP biosynthesis pathways studied so far, tcpC is not able to bishydroxylate the DKP at both alpha-carbon positions, but hydroxylates the alpha-carbon of the tyrosine part and the nitrogen of the glycine part (PubMed:27390873). The next steps involve an alpha,beta-elimination reaction catalyzed by tcpI, a methylation by the methyltransferase tcpN the action of the four enzyme cascade tcpG/K/J/I (PubMed:27390873). Due to a dysfunctional cytochrome P450 monooxygenase tcpC, the pathway leads to the biosynthesis of probable non-toxic metabolites lacking the reactive thiol group (PubMed:27390873).
 tcpN ELISA Kit
 tcpN Recombinant
 tcpN Antibody
 CPUR_02672 ELISA Kit
 CPUR_02672 Recombinant
 CPUR_02672 Antibody
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N-methyltransferase vrtF

 N-methyltransferase vrtF ELISA Kit
 N-methyltransferase vrtF Recombinant
 N-methyltransferase vrtF Antibody
Also known as N-methyltransferase vrtF (Viridicatumtoxin synthesis protein F).
N-methyltransferase; 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 vr
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tA (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).
 vrtF ELISA Kit
 vrtF Recombinant
 vrtF Antibody
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