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Oxidase

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Oxidase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties .

Below are the list of possible Oxidase 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.
 

Oxidase FUB9

 Oxidase FUB9 ELISA Kit
 Oxidase FUB9 Recombinant
 Oxidase FUB9 Antibody
Also known as Oxidase FUB9 (Fusaric acid biosynthesis protein 9).
Oxidase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties (PubMed:25372119). L-aspartate is suggested as fusaric acid amino acid precursor that is activated and further processed to O-acetyl-L-homoserine by
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cluster enzymes aspartate kinase FUB3 and homoserine O-acetyltransferase FUB5, as well as enzymes of the primary metabolism (). The polyketide synthase (PKS) FUB1 generates the triketide trans-2-hexenal which is presumptively released by the hydrolase FUB4 and linked to the NRPS-bound amino acid precursor by NAD(P)-dependent dehydrogenase FUB6 (). FUB1, FUB4, and the non-canonical NRPS Fub8 may form an enzyme complex (). Further processing of the NRPS-bound intermediate might be carried out by FUB6 and the sulfhydrylase FUB7, enabling a spontaneous electrocyclization to close the carbon backbone of fusaric acid (). Dihydrofusaric acid is likely to be released via reduction by the thioester reductase (TR) domain of FUB8 whereupon the final oxidation to fusaric acid may (also) be performed by the FMN-dependent dehydrogenase FUB9 ().
 FUB8 ELISA Kit
 FUB8 Recombinant
 FUB8 Antibody
 FOXG_15238 ELISA Kit
 FOXG_15238 Recombinant
 FOXG_15238 Antibody
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Oxidase ustYa

 Oxidase ustYa ELISA Kit
 Oxidase ustYa Recombinant
 Oxidase ustYa Antibody
Also known as Oxidase ustYa (Ustiloxin B biosynthesis protein Ya).
Oxidase; part of the gene cluster that mediates the biosynthesis of the secondary metabolite ustiloxin B, an antimitotic tetrapeptide (PubMed:24841822, PubMed:27166860, PubMed:26703898). First, ustA is processed by the subtilisin-like endoprotease Kex2 that is outside the ustiloxin B gene cluster, at the C-terminal side of Arg-L
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ys, after transfer to Golgi apparatus through the endoplasmic reticulum (ER) (PubMed:24841822). Cleavage by KEX2 generates 16 peptides YAIG-I to YAIG-XVI (PubMed:24841822). To process the precursor peptide further, at least two peptidases are necessary to cleave the N-terminal and C-terminal sides of the Tyr-Ala-Ile-Gly core peptide which serves as backbone for the synthesis of ustiloxin B, through cyclization and modification of the tyrosine with a non-protein coding amino acid, norvaline (PubMed:24841822). One of the two peptidases must be the serine peptidase ustP; and the other pepdidase is probably ustH (PubMed:24841822). Macrocyclization of the core peptide derived from ustA requires the tyrosinase ustQ, as well as the homologous oxidases ustYa and ustYb, and leads to the production of the first cyclization product N-desmethylustiloxin F (PubMed:27166860, PubMed:26703898). For the formation of N-desmethylustiloxin F, three oxidation steps are required, hydroxylation at the benzylic position, hydroxylation at either the aromatic ring of Tyr or beta-position of Ile, and oxidative cyclization (PubMed:27166860). UstQ may catalyze the oxidation of a phenol moiety, whereas the ustYa and ustYb are most likely responsible for the remaining two-step oxidations (PubMed:27166860). N-desmethylustiloxin F is then methylated by ustM to yield ustiloxin F which in turn substrate of the cytochrome P450 monooxygenase ustC which catalyzes the formation of S-deoxyustiloxin H (PubMed:27166860). The flavoprotein monooxygenases ustF1 and ustF2 then participate in the modification of the side chain of S-deoxyustiloxin H, leading to the synthesis of an oxime intermediate, via ustiloxin H (PubMed:27166860). Finally, carboxylative dehydration performed by the cysteine desulfurase-like protein ustD yields ustiloxin B (PubMed:27166860).
 ustYa ELISA Kit
 ustYa Recombinant
 ustYa Antibody
 AFLA_094990 ELISA Kit
 AFLA_094990 Recombinant
 AFLA_094990 Antibody
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Oxidase ustYb

 Oxidase ustYb ELISA Kit
 Oxidase ustYb Recombinant
 Oxidase ustYb Antibody
Also known as Oxidase ustYb (Ustiloxin B biosynthesis protein Yb).
Oxidase; part of the gene cluster that mediates the biosynthesis of the secondary metabolite ustiloxin B, an antimitotic tetrapeptide (PubMed:24841822, PubMed:27166860, PubMed:26703898). First, ustA is processed by the subtilisin-like endoprotease Kex2 that is outside the ustiloxin B gene cluster, at the C-terminal side of Arg-L
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ys, after transfer to Golgi apparatus through the endoplasmic reticulum (ER) (PubMed:24841822). Cleavage by KEX2 generates 16 peptides YAIG-I to YAIG-XVI (PubMed:24841822). To process the precursor peptide further, at least two peptidases are necessary to cleave the N-terminal and C-terminal sides of the Tyr-Ala-Ile-Gly core peptide which serves as backbone for the synthesis of ustiloxin B, through cyclization and modification of the tyrosine with a non-protein coding amino acid, norvaline (PubMed:24841822). One of the two peptidases must be the serine peptidase ustP; and the other pepdidase is probably ustH (PubMed:24841822). Macrocyclization of the core peptide derived from ustA requires the tyrosinase ustQ, as well as the homologous oxidases ustYa and ustYb, and leads to the production of the first cyclization product N-desmethylustiloxin F (PubMed:27166860, PubMed:26703898). For the formation of N-desmethylustiloxin F, three oxidation steps are required, hydroxylation at the benzylic position, hydroxylation at either the aromatic ring of Tyr or beta-position of Ile, and oxidative cyclization (PubMed:27166860). UstQ may catalyze the oxidation of a phenol moiety, whereas the ustYa and ustYb are most likely responsible for the remaining two-step oxidations (PubMed:27166860). N-desmethylustiloxin F is then methylated by ustM to yield ustiloxin F which in turn substrate of the cytochrome P450 monooxygenase ustC which catalyzes the formation of S-deoxyustiloxin H (PubMed:27166860). The flavoprotein monooxygenases ustF1 and ustF2 then participate in the modification of the side chain of S-deoxyustiloxin H, leading to the synthesis of an oxime intermediate, via ustiloxin H (PubMed:27166860). Finally, carboxylative dehydration performed by the cysteine desulfurase-like protein ustD yields ustiloxin B (PubMed:27166860).
 ustYb ELISA Kit
 ustYb Recombinant
 ustYb Antibody
 AFLA_095020 ELISA Kit
 AFLA_095020 Recombinant
 AFLA_095020 Antibody
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