4.2.3.122: (+)-beta-pinene synthase
This is an abbreviated version!
For detailed information about (+)-beta-pinene synthase, go to the full flat file.
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Synonyms
(+)-pinene cyclase, AvPS, AvTPS1, cyclase III, More, pinene synthase, TPS1
ECTree
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Engineering
Engineering on EC 4.2.3.122 - (+)-beta-pinene synthase
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L423A/S454A
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site-directed mutagenesis, mutation M2, the mutant shows altered substrate specificity and product profile compared to the wild-type enzyme
N345A
N345A/L423A/S454A
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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
N345A/L423A/S454G
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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
N345G/L423A/S454A
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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
S454A
S454G
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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
additional information
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S-limonene synthase is converted to pinene or phellandrene synthases by site-directed mutagenesis, product profiles of mutant enzymes, overview
N345A
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site-directed mutagenesis, the mutation enlarges the active site, the mutant shows altered substrate specificity and product profilecompared to the wild-type enzyme
S454A
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site-directed mutagenesis, the mutation enlarges the active site, the mutant shows altered substrate specificity and product profile compared to the wild-type enzyme