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Aristolochene synthase

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Aristolochene synthase; part of the gene cluster that mediates the biosynthesis of PR-toxin, a bicyclic sesquiterpene belonging to the eremophilane class and acting as a mycotoxin .

Below are the list of possible Aristolochene 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.
 

Aristolochene synthase

 Aristolochene synthase ELISA Kit
 Aristolochene synthase Recombinant
 Aristolochene synthase Antibody
Also known as Aristolochene synthase (AS) (PR-toxin biosynthesis protein 2) (Sesquiterpene cyclase).
Aristolochene synthase; part of the gene cluster that mediates the biosynthesis of PR-toxin, a bicyclic sesquiterpene belonging to the eremophilane class and acting as a mycotoxin (PubMed:24239699, PubMed:26274339). The first step of the pathway is catalyzed by the aristolochene synthase which p
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erforms the cyclization of trans,trans-farnesyl diphosphate (FPP) to the bicyclic sesquiterpene aristolochene (PubMed:8440737, PubMed:15186158, PubMed:24239699). Following the formation of aristolochene, the non-oxygenated aristolochene is converted to the trioxygenated intermediate eremofortin B (PubMed:24239699). This conversion appears to involve three enzymes, a hydroxysterol oxidase-like enzyme, the quinone-oxidase prx3 that forms the quinone-type-structure in the bicyclic nucleus of aristolochene with the C8-oxo group and the C-3 hydroxyl group, and a P450 monooxygenase that introduces the epoxide at the double bond between carbons 1 and 2 (PubMed:24239699). No monoxy or dioxy-intermediates have been reported to be released to the broth, so these three early oxidative reactions may be coupled together (PubMed:24239699). Eremofortin B is further oxidized by another P450 monooxygenase, that introduces a second epoxide between carbons 7 and 11 prior to acetylation to eremofortin A (PubMed:24239699, PubMed:16345540). The second epoxidation may be performed by a second P450 monooxygenase (PubMed:24239699). After the acetylation step, the conversion of eremofortin A to eremofortin C and then to PR-toxin requires only two enzymes (PubMed:24239699). First the conversion of eremofortin A to eremofortin C proceeds by oxidation of the side chain of the molecule at C-12 and is catalyzed by the short-chain oxidoreductase prx1 (PubMed:24239699, PubMed:16345540). The primary alcohol formed by this reaction at C-12 is finally oxidized by the short-chain alcohol dehydrogenase prx4 that forms PR-toxin (PubMed:24239699, PubMed:16345540).
 prx2 ELISA Kit
 prx2 Recombinant
 prx2 Antibody
 ari1 ELISA Kit
 ari1 Recombinant
 ari1 Antibody
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Aristolochene synthase prx2

 Aristolochene synthase prx2 ELISA Kit
 Aristolochene synthase prx2 Recombinant
 Aristolochene synthase prx2 Antibody
Also known as Aristolochene synthase prx2 (AS) (PR-toxin biosynthesis protein 2) (Sesquiterpene cyclase prx2).
Aristolochene synthase; part of the gene cluster that mediates the biosynthesis of PR-toxin, a bicyclic sesquiterpene belonging to the eremophilane class and acting as a mycotoxin (PubMed:24239699). The first step of the pathway is catalyzed by the aristolochene synthase which performs
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the cyclization of trans,trans-farnesyl diphosphate (FPP) to the bicyclic sesquiterpene aristolochene (PubMed:24239699). Following the formation of aristolochene, the non-oxygenated aristolochene is converted to the trioxygenated intermediate eremofortin B (PubMed:24239699). This conversion appears to involve three enzymes, a hydroxysterol oxidase-like enzyme prx7, a quinone-oxidase prx3 that forms the quinone-type-structure in the bicyclic nucleus of aristolochene with the C8-oxo group and the C-3 hydroxyl group, and a P450 monooxygenase (prx8 or prx9) that introduces the epoxide at the double bond between carbons 1 and 2 (PubMed:24239699). No monoxy or dioxy-intermediates have been reported to be released to the broth, so these three early oxidative reactions may be coupled together (PubMed:24239699). Eremofortin B is further oxidized by another P450 monooxygenase, that introduces a second epoxide between carbons 7 and 11 prior to acetylation to eremofortin A (PubMed:24239699). The second epoxidation may be performed by the second P450 monooxygenase in the cluster (prx9), although the substrate specificity of these two P450 enzymes cannot be predicted (PubMed:24239699). The acetylation step is likely performed by the O-acetyltransferase encoded by prx11, the only acetyl transferase in the entire cluster (PubMed:24239699). After the acetylation step, the conversion of eremofortin A to eremofortin C and then to PR-toxin requires only two enzymes (PubMed:24239699). First the conversion of eremofortin A to eremofortin C proceeds by oxidation of the side chain of the molecule at C-12 and is catalyzed by the short-chain oxidoreductase prx1 (PubMed:24239699). The primary alcohol formed by this reaction at C-12 is finally oxidized by the short-chain alcohol dehydrogenase prx4 that forms PR-toxin (PubMed:24239699).
 pxr2 ELISA Kit
 pxr2 Recombinant
 pxr2 Antibody
 Pc12g06310 ELISA Kit
 Pc12g06310 Recombinant
 Pc12g06310 Antibody
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