Isolated from the fungus Coprinus cinereus. The enzyme also forms (+)-delta-cadinene, beta-cubebene, (+)-sativene and traces of several other sequiterpenoids [1-3]. beta-Copaene is formed in the presence of Mg2+ but not Mn2+ . See EC 4.2.3.13, (+)-delta-cadinene synthase, EC 4.2.3.128, beta-cubebene synthase, and EC 4.2.3.129, (+)-sativene synthase.
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The enzyme appears in viruses and cellular organisms
the reaction mechanism requires first the isomerization of all-trans (E,E)-FPP at the 2,3 double bond to generate a cisoid-farnesyl cation. Cop4 then catalyzes a 1,10 ring closure of this farnesyl cation isomer to form the secondary cis-germacrene-dienyl cation. Cop4 generates a tertiary cadinyl cation which upon deprotonation yields its major cyclization product delta-cadinene. The cadinyl cation reacts further to yield other cyclization products beta-cubebene, cubebol, beta-copaene, and sativene
the reaction mechanism requires first the isomerization of all-trans (E,E)-FPP at the 2,3 double bond to generate a cisoid-farnesyl cation. Cop4 then catalyzes a 1,10 ring closure of this farnesyl cation isomer to form the secondary cis-germacrene-dienyl cation. Cop4 generates a tertiary cadinyl cation which upon deprotonation yields its major cyclization product delta-cadinene. The cadinyl cation reacts further to yield other cyclization products beta-cubebene, cubebol, beta-copaene, and sativene
Isolated from the fungus Coprinus cinereus. The enzyme also forms (+)-delta-cadinene, beta-cubebene, (+)-sativene and traces of several other sequiterpenoids [1-3]. beta-Copaene is formed in the presence of Mg2+ but not Mn2+ [2]. See EC 4.2.3.13, (+)-delta-cadinene synthase, EC 4.2.3.128, beta-cubebene synthase, and EC 4.2.3.129, (+)-sativene synthase.
the enzyme accepts (E)-geranyl diphosphate as a substrate, but the catalytic efficiency with the shorter prenyl-diphosphate substrate is lower compared to their longer farnesyl diphosphate substrate
conversion of (E,E)-farnesyl diphosphate proceeds via an (E,E)-germacradienyl carbocation in the case of Cop4. Cyclization of all-trans-farnesyl diphosphate compared to the cyclization of the cis-trans isomer of farnesyl diphosphate serving as a surrogate for the secondary cisoid neryl cation intermediate generated by sesquiterpene synthases capable of isomerizing the C2-C3 bond of all-trans-farnesyl diphosphate. (Z,E)-FPP is cyclized via a (6S)-beta-bisabolene carbocation by Cop4
enzyme CoTPS2 is multifunctional and a terpene synthase that catalyses the synthesis of three sesquiterpenes, beta-ylangene, beta-copaene, and beta-cubebene
Cop4 synthesizes delta-cadinene as its major product, cf. EC 4.2.3.13. Cop4 cultures produce several sesquiterpene compounds betacubebene, sativene, beta-copaene, and cubebol
Cop4 is a catalytically promiscuous enzyme that cyclizes (E,E)-farnesyl diphosphate into multiple products, including (-)-germacrene D and cubebol. But changing the pH of the reaction drastically alters the fidelity of Cop4 and makes it a highly selective enzyme
Escherichia coli strains expressing Cop4 accumulate delta-cadinene as the major terpenoid, accounting for about 40% of the total sesquiterpenes detected
Cop4 synthesizes delta-cadinene as its major product, cf. EC 4.2.3.13. Cop4 cultures produce several sesquiterpene compounds betacubebene, sativene, beta-copaene, and cubebol
Escherichia coli strains expressing Cop4 accumulate delta-cadinene as the major terpenoid, accounting for about 40% of the total sesquiterpenes detected
enzyme CoTPS2 is multifunctional and a terpene synthase that catalyses the synthesis of three sesquiterpenes, beta-ylangene, beta-copaene, and beta-cubebene
Cop4 synthesizes delta-cadinene as its major product, cf. EC 4.2.3.13. Cop4 cultures produce several sesquiterpene compounds betacubebene, sativene, beta-copaene, and cubebol
Cop4 synthesizes delta-cadinene as its major product, cf. EC 4.2.3.13. Cop4 cultures produce several sesquiterpene compounds betacubebene, sativene, beta-copaene, and cubebol
required, enzyme CoTPS2 has the conserved aspartate-rich motif (DDXXD) and NSE/DTE motifs that chelate divalent metal ions, typically Mg2+, in the C-terminal domain
dependent on, two consensus sequences - an aspartate rich DDXXD/E and a NSE/DTE motif - located at the entrance of the active site coordinate a trinuclear Mg2+ cluster. In reactions where Mg2+ is replaced with either Mn2+ or K+ is the disappearance of beta-copaene
lowering the reaction temperature from 25°C to 4°C increases the selectivity of Cop4 for (-)-germacrene D. Increasing the reaction temperature to 37°C has the opposite effect and decreases the fidelity of Cop4. At this temperature Cop4 generates a relative larger fraction of products beta-cubebene, sativene delta-cadinene, and beta-copaene that are derived from a cadinyl cation intermediate
the enzyme expression increases from undeveloped small flowers to mature green flowers, is absent in mature yellow flowers, but very high in flower buds
the enzyme belongs to the terpene sythase superfamily, subfamily TPS-a. The arginine-tryptophan motif, R(R)X8W, present at the N terminus of most mono-TPS and in some sesqui-TPS and di-TPS, is found in CoTPS2. CoTPS2 does not contain a plastid Tp sequence
recombinant CoTPS2 catalyses the synthesis of three compounds, beta-ylangene, beta-copaene, and beta-cubebene, from farnesyl diphosphate. CoTPS2 is a multifunctional beta-ylangene/beta-copaene/beta-cubebene synthase capable of producing three sesquiterpenes, beta-ylangene, beta-copaene, and beta-cubebene. The enzyme is part of the biosynthesis of volatile organic compounds (VOCs) in flowers. Floral scents are a key factor in plant-insect interactions and are vital for successful pollination. The scented flowers of Cananga odorata var. fruticosa are analysed by GC-MS and a total of 49 VOCs are identified at four different stages of flower development. The bulk of these VOCs are terpenes, mainly sesquiterpenes. Enzyme CoTPS2 is a multifunctional terpene synthase that catalyses the synthesis of three sesquiterpenes, beta-ylangene, beta-copaene, and beta-cubebene
the product profile of the wild-type and mutant enzymes is highly dependent on the pH value, the loop mutants show a much larger pH activity range, overview
structural homology modeling of Cop4 using the crystal structure of aristolochene synthase from Aspergillus terreus. Several polar side chains in the H-alpha1 loops of Cop4 and Cop3 move closer to side chains in the metal-binding DDXXD motif
structural homology modeling, hydrogen bond interactions and metal ion coordination in the diphosphate bound closed conformation of the Cop models, overview
site-directed mutagenesis, the mutation converts Cop4 into a much more selective enzyme that produces (-)-germacrene D as the major cyclization product with 50% of total sesquiterpenes products. The mutant makes beta-ylangene, which is a diastereomer of beta-copaene and not synthesized by wild-type Cop4
site-directed mutagenesis, the mutant shows a highly altered product profile compared to the wild-type enzyme with decrease in beta-copaene amounts. Cop4 loop mutant K2331 also becomes more selective for ()-germacrene D under acidic or basic reaction conditions, although less so than the wild-type enzyme
site-directed mutagenesis, the mutation converts Cop4 into a much more selective enzyme that produces (-)-germacrene D as the major cyclization product with 50% of total sesquiterpenes products. The mutant makes beta-ylangene, which is a diastereomer of beta-copaene and not synthesized by wild-type Cop4
gene TPS2, sequence comparisons and phylogenetic analysis and tree, quantitative real-time PCR enzyme expression analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS, transient and functional recombinant expression of YFP-tagged enzyme CoTPS2 in transgenic Nicotiana benthamiana leaves in cytosol under control of CaMV 35S promoter via Agrobacterium tumefaciens-mediated transfection method
The floral transcriptome of ylang ylang (Cananga odorata var. fruticosa) uncovers biosynthetic pathways for volatile organic compounds and a multifunctional and novel sesquiterpene synthase
4.2.3.127 beta-copaene synthase
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