The recombinant enzyme from the plant Arabidopsis thaliana produces 27.3% alpha-barbatene, 17.8% thujopsene (cf. EC 4.2.3.79, thujopsene synthase) and 9.9% beta-chamigrene (cf. EC 4.2.3.78, beta-chamigrene synthase) plus traces of other sesquiterpenoids .
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The enzyme appears in viruses and cellular organisms
The recombinant enzyme from the plant Arabidopsis thaliana produces 27.3% alpha-barbatene, 17.8% thujopsene (cf. EC 4.2.3.79, thujopsene synthase) and 9.9% beta-chamigrene (cf. EC 4.2.3.78, beta-chamigrene synthase) [1] plus traces of other sesquiterpenoids [2].
in vitro catalyses the reaction of geranyl diphosphate to myrcene + limonene + (Z)-beta-ocimene + (E)-beta-ocimene + terpinolene + alpha-terpineol. Formation of these compounds by the enzyme in vivo is rather unlikely, as the protein lacks a transit peptide and is therefore not expected to be present in plastids, where GPP is thought to be produced
the volatile blend from flowers of an T-DNA insertion line contains only group A sesquiterpenes, including (E)-beta-caryophyllene, in similar ratios as the wild type, but none of the group B sesquiterpene compounds
full-length cDNA of At5g44630 expressed in Escherichia coli results in a protein that accepts farnesyl diphosphate as a substrate and converts it into over 15 different sesquiterpenes. The enzymatically formed compounds are identical to the floral group B sesquiterpenes and present in similar ratios as those found in the headspace of Arabidopsis thaliana flowers
method for the recovery of full-length cDNAs from predicted terpene synthase genes containing introns. The approach utilizes Agrobacterium-mediated transient expression coupled with a reverse transcription-polydeoxyribonucleotide chain reaction assay to facilitate expression cloning of processed transcripts. Subsequent expression of intronless cDNAs in a suitable prokaryotic host provides for direct functional testing of the encoded gene product
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4.2.3.69 (+)-alpha-barbatene synthase
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