Cyclase III from Salvia officinalis (sage) gives roughly equal parts of (+)-beta-pinene and (+)-alpha-pinene. See EC 4.2.3.121, (+)-alpha-pinene synthase.
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The enzyme appears in viruses and cellular organisms
Cyclase III from Salvia officinalis (sage) gives roughly equal parts of (+)-beta-pinene and (+)-alpha-pinene. See EC 4.2.3.121, (+)-alpha-pinene synthase.
products are disproportionately high levels of acyclic olefins myrcene and ocimene and monocyclic olefins limonene and terpinolene. Limonene is formed via conformational foldings in addition to the cisoid, anti-endo-pattern
products are disproportionately high levels of acyclic olefins myrcene and ocimene and monocyclic olefins limonene and terpinolene. Limonene is formed via conformational foldings in addition to the cisoid, anti-endo-pattern
products are (+)-alpha-pinene, (+)-camphene, and lesser amounts of (+)-limonene, myrcene, and terpinolene. The bicyclic products of pinene and camphene are derived via the cyclization of the cisoid, anti-endo-conformers of the bound, tertiary allylic intermediate (3R)-linalyl diphosphate. A preassociation mechanism of geranyl diphosphate is suggested in which optimum folding of the terpenyl chain precedes the initial ionization step
reaction proceeds via (3R)-linalyl diphosphate and the (4R)-alpha-terpinyl cation. Products are (+)-alpha-pinene, and lesser amounts of related olefins
stereochemistry is not specified in the publication, reaction of recombinantly expressed S-limonene sythase mutant N345A/L423A/S454A enzyme lacking the N-terminal transit peptide
enzyme removes the C4-proR-hydrogen of the substrate, the C3 proton trans to the dimethyl bridge of the pinyl nucleus, with a stereoselectivity exceeding 94% in the formation of (+)-alpha-pinene
product distribution varies with deuterium substitution at C4 and C10 of substrate. Kinetic isotope effects strongly indicate multiple bicyclic olefin production through the partitioning of common carbocation intermediates
AvPS (AvTPS1) is not responsible for pinene biosynthesis in the seeds of Amomum villosum, no expression of this gene is detected in the seeds, and the expression of AvPS is not in accordance with the accumulation pattern of pinene in the leaves. But alpha-pinene is widely distributed throughout almost the whole plant, i.e. roots, creeping stems, leaves, pericarp, and seeds. beta-Pinene is found in all the tissues, except seeds. Pinene is a naturally occurring constituent of the essential oils in many plant species that has a relevant role in insect repellency and allelopathy (inhibiting root growth of the tested weed species). Gene AvPS is highly expressed in pericarp, the exterior tissue protecting the fruits against biotic stress, AvPS might be the gene involved in biotic defense in Amonum villosum
mutationally converting S-limonene synthase from Mentha spicata (UniProt ID Q9SW76, EC 4.2.3.16) to beta-pinene synthase (EC 4.2.3.122 and 4.2.3.120) or phellandrene synthase (EC 4.2.3.51) reveals the plasticity of the active site
integrative volatile terpenoid profiling and transcriptomics analysis for mining the corresponding genes involved in volatile terpenoid biosynthesis, overview
site-directed mutagenesis, mutation M3 enlarges the active site, the mutant shows altered substrate specificity and product profile compared to the wild-type enzyme, the mutant acts as a pinene synthase and produces about 70% pinenes and has about 2fold increase in the yield of overall terpene products
site-directed mutagenesis, mutation M5, the mutant shows altered substrate specificity and product profile compared to the wild-type enzyme, products of M5 are composed of 9.8% alpha-pinene, 52.7% beta-pinene and 13.4% limonene, it has about 2fold increase in the yield of overall terpene products
site-directed mutagenesis, mutation M4, the mutant shows altered substrate specificity and product profile compared to the wild-type enzyme, products of M4 are composed of 18.81% alpha-pinene, 44.00% beta-pinene, and 16.2% limonene
site-directed mutagenesis, the mutation enlarges the active site, the mutant shows altered substrate specificity and product profile compared to the wild-type enzyme, the mutant enzyme produces about 46% alpha- and beta-pinenes and only about 52% limonene
site-directed mutagenesis, the mutation enlarges the active site, the mutant shows altered substrate specificity and product profilecompared to the wild-type enzyme
site-directed mutagenesis, the mutation enlarges the active site, the mutant shows altered substrate specificity and product profile compared to the wild-type enzyme
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integrative volatile terpenoid profiling and transcriptomics analysis for mining the corresponding genes involved in volatile terpenoid biosynthesis, overview
Wang, H.; Ma, D.; Yang, J.; Deng, K.; Li, M.; Ji, X.; Zhong, L.; Zhao, H.
An integrative volatile terpenoid profiling and transcriptomics analysis for gene mining and functional characterization of AvBPPS and AvPS involved in the monoterpenoid biosynthesis in Amomum villosum