The role of aristolochene synthase in diphosphate activation.
نویسندگان
چکیده
Analysis of the role of amino acids involved in diphosphate binding in the Michaelis complex of aristolochene synthase from P. roqueforti (PR-AS) reveals mechanistic details about leaving group (PPi) activation and the nature of the active site acid.
منابع مشابه
Probing the reaction mechanism of aristolochene synthase with 12,13-difluorofarnesyl diphosphate.
12,13-Difluorofarnesyl diphosphate, prepared using Suzuki-Miyaura chemistry, is a potent inhibitor of aristolochene synthase (AS), indicating that the initial cyclisation during AS catalysis generates germacryl cation in a concerted reaction.
متن کاملTemplating effects in aristolochene synthase catalysis: elimination versus cyclisation.
Analysis of the products generated by mutants of aristolochene synthase from P. roqueforti (PR-AS) revealed the prominent structural role played by the aliphatic residue Leu 108 in maintaining the productive conformation of farnesyl diphosphate to ensure C1-C10 (σ-bond) ring-closure and hence (+)-aristolochene production.
متن کاملFusion of farnesyldiphosphate synthase and epi-aristolochene synthase, a sesquiterpene cyclase involved in capsidiol biosynthesis in Nicotiana tabacum.
A clone encoding farnesyl diphosphate synthase (FPPS) was obtained by PCR from a cDNA library made from young leaves of Artemisia annua. A cDNA clone encoding the tobacco epi-aristolochene synthase (eAS) was kindly supplied by J. Chappell (University of Kentucky, Lexington, KY, USA). Two fusions were constructed, i.e. FPPS/eAS and eAS/FPPS. The stop codon of the N-terminal enzyme was removed an...
متن کاملEnzymatic synthesis of natural (+)-aristolochene from a non-natural substrate.
The sesquiterpene cyclase aristolochene synthase from Penicillium roquefortii (PR-AS) has evolved to catalyse with high specificity (92%) the conversion of farnesyl diphosphate (FDP) to the bicyclic hydrocarbon (+)-aristolochene, the natural precursor of several fungal toxins. Here we report that PR-AS converts the unnatural FDP isomer 7-methylene farnesyl diphosphate to (+)-aristolochene via t...
متن کاملThe cyclization of farnesyl diphosphate and nerolidyl diphosphate by a purified recombinant delta-cadinene synthase.
The first step in the conversion of the isoprenoid intermediate, farnesyl diphosphate (FDP), to sesquiterpene phytoalexins in cotton (Gossypium barbadense) plants is catalyzed by delta-cadinene (CDN) synthase. CDN is the precursor of desoxyhemigossypol and hemigossypol defense sesquiterpenes. In this paper we have studied the mechanism for the cyclization of FDP and the putative intermediate, n...
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ورودعنوان ژورنال:
- Chemical communications
دوره 48 26 شماره
صفحات -
تاریخ انتشار 2012