t-muurolol and farnesyl-pyrophosphate

t-muurolol has been researched along with farnesyl-pyrophosphate* in 1 studies

Other Studies

1 other study(ies) available for t-muurolol and farnesyl-pyrophosphate

Article	Year
Genome mining in Streptomyces clavuligerus: expression and biochemical characterization of two new cryptic sesquiterpene synthases. Chemistry & biology, 2011, Jan-28, Volume: 18, Issue:1 Two presumptive terpene synthases of unknown biochemical function encoded by the sscg_02150 and sscg_03688 genes of Streptomyces clavuligerus ATCC 27074 were individually expressed in Escherichia coli as N-terminal-His₆-tag proteins, using codon-optimized synthetic genes. Incubation of recombinant SSCG_02150 with farnesyl diphosphate (1, FPP) gave (-)-δ-cadinene (2) while recombinant SSCG_03688 converted FPP to (+)-T-muurolol (3). Individual incubations of (-)-δ-cadinene synthase with [1,1-²H₂]FPP (1a), (1S)-[1-²H]-FPP (1b), and (1R)-[1-²H]-FPP (1c) and NMR analysis of the resulting samples of deuterated (-)-δ-cadinene supported a cyclization mechanism involving the intermediacy of nerolidyl diphosphate (4) leading to a helminthogermacradienyl cation 5. Following a 1,3-hydride shift of the original H-1(si) of FPP, cyclization and deprotonation will give (-)-δ-cadinene. Similar incubations with recombinant SSCG_03688 supported an analogous mechanism for the formation of (+)-T-muurolol (3), also involving a 1,3-hydride shift of the original H-1(si) of FPP. Topics: Alkyl and Aryl Transferases; Biocatalysis; Cyclization; Escherichia coli; Gene Expression; Genome, Bacterial; Genomics; Kinetics; Polycyclic Sesquiterpenes; Polyisoprenyl Phosphates; Protein Engineering; Recombinant Proteins; Sesquiterpenes; Stereoisomerism; Streptomyces; Terpenes	2011

Article

Year

Genome mining in Streptomyces clavuligerus: expression and biochemical characterization of two new cryptic sesquiterpene synthases.

Chemistry & biology, 2011, Jan-28, Volume: 18, Issue:1

Two presumptive terpene synthases of unknown biochemical function encoded by the sscg_02150 and sscg_03688 genes of Streptomyces clavuligerus ATCC 27074 were individually expressed in Escherichia coli as N-terminal-His₆-tag proteins, using codon-optimized synthetic genes. Incubation of recombinant SSCG_02150 with farnesyl diphosphate (1, FPP) gave (-)-δ-cadinene (2) while recombinant SSCG_03688 converted FPP to (+)-T-muurolol (3). Individual incubations of (-)-δ-cadinene synthase with [1,1-²H₂]FPP (1a), (1S)-[1-²H]-FPP (1b), and (1R)-[1-²H]-FPP (1c) and NMR analysis of the resulting samples of deuterated (-)-δ-cadinene supported a cyclization mechanism involving the intermediacy of nerolidyl diphosphate (4) leading to a helminthogermacradienyl cation 5. Following a 1,3-hydride shift of the original H-1(si) of FPP, cyclization and deprotonation will give (-)-δ-cadinene. Similar incubations with recombinant SSCG_03688 supported an analogous mechanism for the formation of (+)-T-muurolol (3), also involving a 1,3-hydride shift of the original H-1(si) of FPP.

Topics: Alkyl and Aryl Transferases; Biocatalysis; Cyclization; Escherichia coli; Gene Expression; Genome, Bacterial; Genomics; Kinetics; Polycyclic Sesquiterpenes; Polyisoprenyl Phosphates; Protein Engineering; Recombinant Proteins; Sesquiterpenes; Stereoisomerism; Streptomyces; Terpenes

2011