Requires Mg2+. Isolated from the bacterium Streptomyces sp. SANK 60404. This trifunctional enzyme, which contains a [4Fe-4S] cluster, also produces (R)-nephthenol and (1S,4E,8E,12E)-2,2,5,9,13-pentamethylcyclopentadeca-4,8,12-trien-1-ol. See EC 4.2.3.149, nephthenol synthase and EC 4.2.3.151, pentamethylcyclopentadecatrienol synthase.
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
gene name. The trifunctional enzyme also produces (R)-nephthenol and (1S,4E,8E,12E)-2,2,5,9,13-pentamethylcyclopentadeca-4,8,12-trien-1-ol. See EC 4.2.3.149, nephthenol synthase and EC 4.2.3.151, pentamethylcyclopentadecatrienol synthase
gene name. The trifunctional enzyme also produces (R)-nephthenol and (1S,4E,8E,12E)-2,2,5,9,13-pentamethylcyclopentadeca-4,8,12-trien-1-ol. See EC 4.2.3.149, nephthenol synthase and EC 4.2.3.151, pentamethylcyclopentadecatrienol synthase
geranylgeranyl diphosphate = (R)-cembrene A + diphosphate
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geranylgeranyl diphosphate = (R)-cembrene A + diphosphate
the cyclization mechanism from geranylgeranyl diphosphate to cembrene A requires a 1,14-cyclization to the ent-cembranyl cation and deprotonation of one of the geminal methyl groups, reaction mechanism, overview
geranylgeranyl diphosphate = (R)-cembrene A + diphosphate
the cyclization mechanism from geranylgeranyl diphosphate to cembrene A requires a 1,14-cyclization to the ent-cembranyl cation and deprotonation of one of the geminal methyl groups, reaction mechanism, overview
Requires Mg2+. Isolated from the bacterium Streptomyces sp. SANK 60404. This trifunctional enzyme, which contains a [4Fe-4S] cluster, also produces (R)-nephthenol and (1S,4E,8E,12E)-2,2,5,9,13-pentamethylcyclopentadeca-4,8,12-trien-1-ol. See EC 4.2.3.149, nephthenol synthase and EC 4.2.3.151, pentamethylcyclopentadecatrienol synthase.
the trifunctional enzyme also produces (R)-nephthenol and (1S,4E,8E,12E)-2,2,5,9,13-pentamethylcyclopentadeca-4,8,12-trien-1-ol. See EC 4.2.3.149, nephthenol synthase and EC 4.2.3.151, pentamethylcyclopentadecatrienol synthase
the trifunctional enzyme also produces (R)-nephthenol and (1S,4E,8E,12E)-2,2,5,9,13-pentamethylcyclopentadeca-4,8,12-trien-1-ol. See EC 4.2.3.149, nephthenol synthase and EC 4.2.3.151, pentamethylcyclopentadecatrienol synthase
product identification by NMR spectroscopic analysis. Development of a method that uses the stereoselectively deuterated precursors (S)- and (R)-(1-13C,1-2H)farnesyl diphosphate and (S)- and (R)-(1-13C,1-2H)geranyl diphosphate to determine the absolute configurations of terpenes
product identification by NMR spectroscopic analysis. Development of a method that uses the stereoselectively deuterated precursors (S)- and (R)-(1-13C,1-2H)farnesyl diphosphate and (S)- and (R)-(1-13C,1-2H)geranyl diphosphate to determine the absolute configurations of terpenes
site-directed mutagenesis, the mutant follows a different reaction mechanism compared to wild-type and produces the different product cembrane A instead of cyclooctat-9-en-7-ol
site-directed mutagenesis, the mutant follows a different reaction mechanism compared to wild-type and produces the different products cembrane A and 3,7,18-dolabellatriene and only low amounts of cyclooctat-9-en-7-ol
site-directed mutagenesis, the mutant follows a different reaction mechanism compared to wild-type and produces the different product cembrane A instead of cyclooctat-9-en-7-ol
site-directed mutagenesis, the mutant follows a different reaction mechanism compared to wild-type and produces the different products cembrane A and 3,7,18-dolabellatriene and only low amounts of cyclooctat-9-en-7-ol
the mutation leads to the exclusive formation of side product cembrene A. The simulations of the W753H mutant shows that, in the mutant structure, the His side chain is in the perfect position to deprotonate the cembrenyl cation en route to cembrene formation and that this abortive deprotonation is an energetically facile process
mutational analysis of the atypical aspartate-rich motif of CotB2 (EC 4.2.3.146). The substrate specificity of the CotB2 mutants can be completely changed. Proposed cyclization mechanism for CotB2 and its mutants, overview
mutational analysis of the atypical aspartate-rich motif of CotB2 (EC 4.2.3.146). The substrate specificity of the CotB2 mutants can be completely changed. Proposed cyclization mechanism for CotB2 and its mutants, overview