the BmeTC-catalyzed reaction of the substrate is initiated by the protonation of a terminal isopropylidene moiety, triggering a series of cyclization events, erminated by the nucleophilic addition of a hydroxyl group or the deprotonation of H-26 at the resulting C-8 carbocation, respectively
Bcl-TS is a sesterterpene (C25)/triterpene (C30) synthase, the enzyme catalyzes the conversion of (all-E)-geranylfarnesyl diphosphate (GFPP) and (all-E)-hexaprenyl diphosphate (HexPP) into beta-geranylfarnesene and beta-hexaprene in a head-to-tail triterpene synthase. NMR spectroscopic and TLC analysis of radiolabeled products, overview. Enzyme Bcl-TS can accept HepPP (C35) as a substrate and cyclizes HepPP (C35) to a monocycle
onoceroids are synthesized from squalene via an intermediate cyclized from one terminus, such as 8alpha-hydroxypolypoda-13,17,21-triene, by cyclization at both termini. Enzyme BmeTC may have single active site: it starts with the initial cascade leading to the bicyclic intermediate 8alpha-hydroxypolypoda-13,17,21-triene from squalene, then turns molecule 8alpha-hydroxypolypoda-13,17,21-triene outside of the active site cavity, and again uptake 8alpha-hydroxypolypoda-13,17,21-triene to catalyze the formation of additional bicyclic and tricyclic structures of onoceranoxide and 14beta-hydroxyonocera-8(26)-ene on the other side of 8alpha-hydroxypolypoda-13,17,21-triene. BmeTC is not only a bifunctional terpene cyclase which converts tetraprenyl-beta-curcumene and squalene into baciterpenol A and 8alpha-hydroxypolypoda-13,17,21-triene but also an onoceroid synthase that catalyzes the convertion of 8alpha-hydroxypolypoda-13,17,21-triene into onoceranoxide and 14beta-hydroxyonocera-8(26)-ene. GC-MS product analysis, overview
GFPP and HexPP, the enzyme Bcl-TS substrates, are biosynthesized by enzymes E-IDS2-S/L in Bacillus clausii, and the tetraprenyl-beta-curcumene cyclase forms baciterpenol A from tetraprenyl-beta-curcumene. Proposed pathways for the biosynthesis of acyclic terpenes and menaquinones by Bacillus clausii, overview
the tetraprenyl-beta-curcumene synthase homologue from Bacillus clausii (Bcl-TS) catalyzes the conversion of (all-E)-geranylfarnesyl diphosphate (GFPP) and (all-E)-hexaprenyl diphosphate (HexPP) into beta-geranylfarnesene and beta-hexaprene, respectively, in vitro, and both compounds are produced in Bacillus clausii. THe enzyme is involved in the biosynthesis of menaquinones
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gene ytpB, expression as fusion protein in Escherichia coli strain BL21(DE3) from pColdTF. The ts gene or ytpB gene forms an operon with a lysophospholipase gene ytpA, which is responsible for the biosynthesis of the antibiotic bacilysocin in Bacillus subtilis
Sato, T.; Yoshida, S.; Hoshino, H.; Tanno, M.; Nakajima, M.; Hoshino, T.
Sesquarterpenes (C35 terpenes) biosynthesized via the cyclization of a linear C35 isoprenoid by a tetraprenyl-beta-curcumene synthase and a tetraprenyl-beta-curcumene cyclase: identification of a new terpene cyclase