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Nonribosomal peptide synthetase

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Nonribosomal peptide synthesis (NRPS) is a key mechanism responsible for the biosynthesis of bioactive metabolites which are potentially contributing to organismal virulence. Contributes to improved fungal tolerance against oxidative stress, during the infection process.

Below are the list of possible Nonribosomal peptide synthetase 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.
 

Nonribosomal peptide synthetase 1

 Nonribosomal peptide synthetase 1 ELISA Kit
 Nonribosomal peptide synthetase 1 Recombinant
 Nonribosomal peptide synthetase 1 Antibody
Nonribosomal peptide synthesis (NRPS) is a key mechanism responsible for the biosynthesis of bioactive metabolites which are potentially contributing to organismal virulence. Contributes to improved fungal tolerance against oxidative stress, during the infection process.
 NRPS1 ELISA Kit
 NRPS1 Recombinant
 NRPS1 Antibody
 pes1 ELISA Kit
 pes1 Recombinant
 pes1 Antibody
 pesB ELISA Kit
 pesB Recombinant
 pesB Antibody
 AFUA_1G10380 ELISA Kit
 AFUA_1G10380 Recombinant
 AFUA_1G10380 Antibody
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Nonribosomal peptide synthetase 11

 Nonribosomal peptide synthetase 11 ELISA Kit
 Nonribosomal peptide synthetase 11 Recombinant
 Nonribosomal peptide synthetase 11 Antibody
Nonribosomal peptide synthesis (NRPS) is a key mechanism responsible for the biosynthesis of bioactive metabolites which are potentially contributing to organismal virulence. Involved in the conversion of fumiquinazoline F (FQF) to fumiquinazoline A (FQA). After oxidation of the 2',3'-double bond of the indole side chain of FQF by AFUA_6G12060, NRPS11 activates L-Ala as the adenylate, installs it as the pantetheinyl thioester on its carrier protein domain and acylates the oxidized indole for subsequent intramolecular cyclization to create the 6-5-5 imidazolindolone of FQA.
 NRPS11 ELISA Kit
 NRPS11 Recombinant
 NRPS11 Antibody
 pesL ELISA Kit
 pesL Recombinant
 pesL Antibody
 AFUA_6G12050 ELISA Kit
 AFUA_6G12050 Recombinant
 AFUA_6G12050 Antibody
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Nonribosomal peptide synthetase 12

 Nonribosomal peptide synthetase 12 ELISA Kit
 Nonribosomal peptide synthetase 12 Recombinant
 Nonribosomal peptide synthetase 12 Antibody
Nonribosomal peptide synthesis (NRPS) is a key mechanism responsible for the biosynthesis of bioactive metabolites which are potentially contributing to organismal virulence. Involved in the synthesis of fumiquinazoline F (FQF).
 NRPS12 ELISA Kit
 NRPS12 Recombinant
 NRPS12 Antibody
 pesM ELISA Kit
 pesM Recombinant
 pesM Antibody
 AFUA_6G12080 ELISA Kit
 AFUA_6G12080 Recombinant
 AFUA_6G12080 Antibody
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Nonribosomal peptide synthetase 13

 Nonribosomal peptide synthetase 13 ELISA Kit
 Nonribosomal peptide synthetase 13 Recombinant
 Nonribosomal peptide synthetase 13 Antibody
Also known as Nonribosomal peptide synthetase 13 (Brevianamide F synthase) (Fumitremorgin biosynthesis protein A).
Catalyzes the condensation of L-tryptophan and L-proline to produce brevianamide F (). Nonribosomal peptide synthesis (NRPS) is a key mechanism responsible for the biosynthesis of bioactive metabolites which are potentially contributing to organismal virulence.
 NRPS13 ELISA Kit
 NRPS13 Recombinant
 NRPS13 Antibody
 ftmA ELISA Kit
 ftmA Recombinant
 ftmA Antibody
 pesN ELISA Kit
 pesN Recombinant
 pesN Antibody
 AFUA_8G00170 ELISA Kit
 AFUA_8G00170 Recombinant
 AFUA_8G00170 Antibody
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Nonribosomal peptide synthetase 2

 Nonribosomal peptide synthetase 2 ELISA Kit
 Nonribosomal peptide synthetase 2 Recombinant
 Nonribosomal peptide synthetase 2 Antibody
Also known as Nonribosomal peptide synthetase 2 (Siderophore peptide synthase C).
Nonribosomal peptide synthesis (NRPS) is a key mechanism responsible for the biosynthesis of bioactive metabolites which are potentially contributing to organismal virulence. Involved in the synthesis of siderophore ferricrocin. Siderophore biosynthesis commences with the N5-hydroxylation of ornithine, followed by transacylation and subsequent covalent assembly of the modified ornithine residues with or without further amino acids (such as serine, alanine and glycine).
 NRPS2 ELISA Kit
 NRPS2 Recombinant
 NRPS2 Antibody
 sidC ELISA Kit
 sidC Recombinant
 sidC Antibody
 AFUA_1G17200 ELISA Kit
 AFUA_1G17200 Recombinant
 AFUA_1G17200 Antibody
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Nonribosomal peptide synthetase 3

 Nonribosomal peptide synthetase 3 ELISA Kit
 Nonribosomal peptide synthetase 3 Recombinant
 Nonribosomal peptide synthetase 3 Antibody
Also known as Nonribosomal peptide synthetase 3 (Siderophore peptide synthase E).
Nonribosomal peptide synthesis (NRPS) is a key mechanism responsible for the biosynthesis of bioactive metabolites which are potentially contributing to organismal virulence. Involved in the synthesis of siderophores. Siderophore biosynthesis commences with the N5-hydroxylation of ornithine, followed by transacylation and subsequent covalent assembly of the modified ornithine residues with or without further amino acids (such as serine, alanine and glycine).
 NRPS3 ELISA Kit
 NRPS3 Recombinant
 NRPS3 Antibody
 sidE ELISA Kit
 sidE Recombinant
 sidE Antibody
 AFUA_3G03350 ELISA Kit
 AFUA_3G03350 Recombinant
 AFUA_3G03350 Antibody
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Nonribosomal peptide synthetase 4

 Nonribosomal peptide synthetase 4 ELISA Kit
 Nonribosomal peptide synthetase 4 Recombinant
 Nonribosomal peptide synthetase 4 Antibody
Also known as Nonribosomal peptide synthetase 4 (Siderophore peptide synthase D).
Nonribosomal peptide synthesis (NRPS) is a key mechanism responsible for the biosynthesis of bioactive metabolites which are potentially contributing to organismal virulence. Involved in the synthesis of siderophore triacetylfusarinine C (TAFC). Siderophore biosynthesis commences with the N5-hydroxylation of ornithine, followed by transacylation and subsequent covalent assembly of the modified ornithine residues with or without further amino acids (such as serine, alanine and glycine).
 NRPS4 ELISA Kit
 NRPS4 Recombinant
 NRPS4 Antibody
 nps6 ELISA Kit
 nps6 Recombinant
 nps6 Antibody
 sidD ELISA Kit
 sidD Recombinant
 sidD Antibody
 AFUA_3G03420 ELISA Kit
 AFUA_3G03420 Recombinant
 AFUA_3G03420 Antibody
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Nonribosomal peptide synthetase 5

 Nonribosomal peptide synthetase 5 ELISA Kit
 Nonribosomal peptide synthetase 5 Recombinant
 Nonribosomal peptide synthetase 5 Antibody
Nonribosomal peptide synthesis (NRPS) is a key mechanism responsible for the biosynthesis of bioactive metabolites which are potentially contributing to organismal virulence.
 NRPS5 ELISA Kit
 NRPS5 Recombinant
 NRPS5 Antibody
 pesF ELISA Kit
 pesF Recombinant
 pesF Antibody
 AFUA_3G12920 ELISA Kit
 AFUA_3G12920 Recombinant
 AFUA_3G12920 Antibody
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Nonribosomal peptide synthetase 6

 Nonribosomal peptide synthetase 6 ELISA Kit
 Nonribosomal peptide synthetase 6 Recombinant
 Nonribosomal peptide synthetase 6 Antibody
Nonribosomal peptide synthesis (NRPS) is a key mechanism responsible for the biosynthesis of bioactive metabolites which are potentially contributing to organismal virulence.
 NRPS6 ELISA Kit
 NRPS6 Recombinant
 NRPS6 Antibody
 pesG ELISA Kit
 pesG Recombinant
 pesG Antibody
 AFUA_3G13730 ELISA Kit
 AFUA_3G13730 Recombinant
 AFUA_3G13730 Antibody
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Nonribosomal peptide synthetase 7

 Nonribosomal peptide synthetase 7 ELISA Kit
 Nonribosomal peptide synthetase 7 Recombinant
 Nonribosomal peptide synthetase 7 Antibody
Nonribosomal peptide synthesis (NRPS) is a key mechanism responsible for the biosynthesis of bioactive metabolites which are potentially contributing to organismal virulence.
 NRPS7 ELISA Kit
 NRPS7 Recombinant
 NRPS7 Antibody
 pesH ELISA Kit
 pesH Recombinant
 pesH Antibody
 AFUA_3G15270 ELISA Kit
 AFUA_3G15270 Recombinant
 AFUA_3G15270 Antibody
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Nonribosomal peptide synthetase 8

 Nonribosomal peptide synthetase 8 ELISA Kit
 Nonribosomal peptide synthetase 8 Recombinant
 Nonribosomal peptide synthetase 8 Antibody
Nonribosomal peptide synthesis (NRPS) is a key mechanism responsible for the biosynthesis of bioactive metabolites which are potentially contributing to organismal virulence. However, contarary to other nonribosomal peptide synthases, NRPS8 does not encode a secreted peptide, but has more a structural role since it is involved in germ tube formation.
 NRPS8 ELISA Kit
 NRPS8 Recombinant
 NRPS8 Antibody
 pes3 ELISA Kit
 pes3 Recombinant
 pes3 Antibody
 pesI ELISA Kit
 pesI Recombinant
 pesI Antibody
 AFUA_5G12730 ELISA Kit
 AFUA_5G12730 Recombinant
 AFUA_5G12730 Antibody
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Nonribosomal peptide synthetase asqK

 Nonribosomal peptide synthetase asqK ELISA Kit
 Nonribosomal peptide synthetase asqK Recombinant
 Nonribosomal peptide synthetase asqK Antibody
Also known as Nonribosomal peptide synthetase asqK (NRPS asqK) (4'-methoxyviridicatin/aspoquinolone biosynthesis cluster protein asqK) (Aspoquinolone biosynthesis protein K).
Nonribosomal peptide synthetase; 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 cond
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enses anthranilic acid 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).
 asqK ELISA Kit
 asqK Recombinant
 asqK Antibody
 AN9226 ELISA Kit
 AN9226 Recombinant
 AN9226 Antibody
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Nonribosomal peptide synthetase dtxS1

 Nonribosomal peptide synthetase dtxS1 ELISA Kit
 Nonribosomal peptide synthetase dtxS1 Recombinant
 Nonribosomal peptide synthetase dtxS1 Antibody
Also known as Nonribosomal peptide synthetase dtxS1 (Destruxin synthase dtxS1) (DXS) (Destruxin synthesis protein 1).
Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of destruxins, insecticidal cyclic hexadepsipeptides which induce flaccid paralysis and visceral muscle contraction in insects through targeting the calcium channels and vacuolar-type ATPase
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s (PubMed:22367459, PubMed:22232661). The aldo-keto reductase dtxS3 converts alpha-ketoisocaproic acid from deaminated leucine into alpha-hydroxyisocaproic acid (HIC), which is the first substrate for destruxin assembly by dtxS1 (PubMed:22232661). L-aspartate decarboxylase dtxS4 converts aspartic acid into beta-alanine, the last substrate for the destruxin assembly line performed by dtxS1 (PubMed:22232661). The nonribosomal peptide synthetase dtxS1 synthesizes destruxins B and B2, whereas the cytochrome P450 monooxygenase dtxS2 is required to convert destruxin B into other destruxin derivatives, including destructins C, D, A and E (PubMed:22232661). Destruxin E-diol (ED) is further produced in a non-enzymatic manner from destruxin E (PubMed:22232661). Destruxins play an important role in virulence and escape from insect host immune defenses (PubMed:22232661).
 dtxS1 ELISA Kit
 dtxS1 Recombinant
 dtxS1 Antibody
 MAA_10043 ELISA Kit
 MAA_10043 Recombinant
 MAA_10043 Antibody
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Nonribosomal peptide synthetase gliP

 Nonribosomal peptide synthetase gliP ELISA Kit
 Nonribosomal peptide synthetase gliP Recombinant
 Nonribosomal peptide synthetase gliP Antibody
Also known as Nonribosomal peptide synthetase gliP (NRPS gliP) (Gliotoxin biosynthesis protein P).
Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of gliotoxin, a member of the epipolythiodioxopiperazine (ETP) class of toxins characterized by a disuldide bridged cyclic dipeptide (PubMed:15979823, PubMed:16757745, PubMed:16956378, PubMed:21612254). The first step in gliotoxin biosynthesis is the condensation of serine and phenylalanine to form the cyclo-L-phenylalanyl-L-serine diketopiperazine (DKP) by the NRPS gliP (PubMed:17154540, PubMed:21612254).
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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).
 gliP ELISA Kit
 gliP Recombinant
 gliP Antibody
 NRPS10 ELISA Kit
 NRPS10 Recombinant
 NRPS10 Antibody
 pesK ELISA Kit
 pesK Recombinant
 pesK Antibody
 AFUA_6G09660 ELISA Kit
 AFUA_6G09660 Recombinant
 AFUA_6G09660 Antibody
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Nonribosomal peptide synthetase sirP

 Nonribosomal peptide synthetase sirP ELISA Kit
 Nonribosomal peptide synthetase sirP Recombinant
 Nonribosomal peptide synthetase sirP Antibody
Also known as Nonribosomal peptide synthetase sirP (NRPS sirP) (Sirodesmin biosynthesis protein P).
Nonribosomal peptide synthetase; 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,
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PubMed:18272357, PubMed:19762440). SirD 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).
 sirP ELISA Kit
 sirP Recombinant
 sirP Antibody
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Nonribosomal peptide synthetase tcpP

 Nonribosomal peptide synthetase tcpP ELISA Kit
 Nonribosomal peptide synthetase tcpP Recombinant
 Nonribosomal peptide synthetase tcpP Antibody
Also known as Nonribosomal peptide synthetase tcpP (NRPS tcpP) (Thioclapurine biosynthesis protein P).
Nonribosomal peptide synthetase; 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 condensatio
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n with L-glycine in a reaction catalyzed 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).
 tcpP ELISA Kit
 tcpP Recombinant
 tcpP Antibody
 CPUR_02680 ELISA Kit
 CPUR_02680 Recombinant
 CPUR_02680 Antibody
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