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Literature summary extracted from

  • Xu, J.; Ai, Y.; Wang, J.; Xu, J.; Zhang, Y.; Yang, D.
    Converting S-limonene synthase to pinene or phellandrene synthases reveals the plasticity of the active site (2017), Phytochemistry, 137, 34-41 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.3.120 recombinant expression of GST-tagged S-limonene synthase mutant in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha Mentha spicata
4.2.3.122 recombinant expression of GST-tagged S-limonene synthase mutant in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha Mentha spicata

Protein Variants

EC Number Protein Variants Comment Organism
4.2.3.120 H579A site-directed mutagenesis, the mutant produces only 56.3% S-limonene Mentha spicata
4.2.3.120 L423A/S454A site-directed mutagenesis, mutation M2, the mutant shows altered substrate specificity and product profile compared to the wild-type enzyme Mentha spicata
4.2.3.120 M458A site-directed mutagenesis, the mutant produces only 3.2% S-limonene Mentha spicata
4.2.3.120 additional information S-limonene synthase is converted to pinene or phellandrene synthases by site-directed mutagenesis, product profiles of mutant enzymes, overview Mentha spicata
4.2.3.120 N345A site-directed mutagenesis, the mutant produces only 20.9%imonene Mentha spicata
4.2.3.120 N345A site-directed mutagenesis, the mutation enlarges the active site, the mutant shows altered substrate specificity and product profilecompared to the wild-type enzyme Mentha spicata
4.2.3.120 N345A/L423A/S454A 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 Mentha spicata
4.2.3.120 N345A/L423A/S454G 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 Mentha spicata
4.2.3.120 N345G/L423A/S454A 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 Mentha spicata
4.2.3.120 S454A site-directed mutagenesis, the mutant produces only 73.7% S-limonene Mentha spicata
4.2.3.120 S454A site-directed mutagenesis, the mutation enlarges the active site, the mutant shows altered substrate specificity and product profile compared to the wild-type enzyme Mentha spicata
4.2.3.120 S454G 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 Mentha spicata
4.2.3.120 T349A site-directed mutagenesis, the mutant produces only 60.3% limonene Mentha spicata
4.2.3.120 W324A site-directed mutagenesis, the mutant produces only 18.1% S-limonene Mentha spicata
4.2.3.122 H579A site-directed mutagenesis, the mutant produces only 56.3% S-limonene Mentha spicata
4.2.3.122 L423A/S454A site-directed mutagenesis, mutation M2, the mutant shows altered substrate specificity and product profile compared to the wild-type enzyme Mentha spicata
4.2.3.122 M458A site-directed mutagenesis, the mutant produces only 3.2% S-limonene Mentha spicata
4.2.3.122 additional information S-limonene synthase is converted to pinene or phellandrene synthases by site-directed mutagenesis, product profiles of mutant enzymes, overview Mentha spicata
4.2.3.122 N345A site-directed mutagenesis, the mutant produces only 20.9%imonene Mentha spicata
4.2.3.122 N345A site-directed mutagenesis, the mutation enlarges the active site, the mutant shows altered substrate specificity and product profilecompared to the wild-type enzyme Mentha spicata
4.2.3.122 N345A/L423A/S454A 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 Mentha spicata
4.2.3.122 N345A/L423A/S454G 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 Mentha spicata
4.2.3.122 N345G/L423A/S454A 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 Mentha spicata
4.2.3.122 S454A site-directed mutagenesis, the mutant produces only 73.7% S-limonene Mentha spicata
4.2.3.122 S454A site-directed mutagenesis, the mutation enlarges the active site, the mutant shows altered substrate specificity and product profile compared to the wild-type enzyme Mentha spicata
4.2.3.122 S454G 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 Mentha spicata
4.2.3.122 T349A site-directed mutagenesis, the mutant produces only 60.3% limonene Mentha spicata
4.2.3.122 W324A site-directed mutagenesis, the mutant produces only 18.1% S-limonene Mentha spicata

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
4.2.3.120 chloroplast
-
 Mentha spicata 9507
-
4.2.3.122 chloroplast
-
 Mentha spicata 9507
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.2.3.120 Mg2+ required Mentha spicata
4.2.3.122 Mg2+ required Mentha spicata

Organism

EC Number Organism UniProt Comment Textmining
4.2.3.120 Mentha spicata
-
-
-
4.2.3.122 Mentha spicata
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.3.120 recombinant GST-tagged S-limonene synthase mutant from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography Mentha spicata
4.2.3.122 recombinant GST-tagged S-limonene synthase mutant from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography Mentha spicata

Source Tissue

EC Number Source Tissue Comment Organism Textmining
4.2.3.120 leaf
-
 Mentha spicata
-
4.2.3.122 leaf
-
 Mentha spicata
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.3.120 geranyl diphosphate stereochemistry of the product is not specified in the publication, reaction of recombinantly expressed S-limonene sythase mutant N345A/L423A/S454A enzyme lacking the N-terminal transit peptide Mentha spicata beta-pinene + diphosphate
-
 ?
4.2.3.120 additional information product profiles of mutant enzymes, overview Mentha spicata ?
-
 ?
4.2.3.122 geranyl diphosphate 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 Mentha spicata beta-pinene + diphosphate
-
 ?
4.2.3.122 additional information product profiles of mutant enzymes, overview Mentha spicata ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.2.3.120 More cf. EC 4.2.3.122 Mentha spicata
4.2.3.120 pinene synthase
-
 Mentha spicata
4.2.3.122 More cf. EC 4.2.3.120 Mentha spicata
4.2.3.122 pinene synthase
-
 Mentha spicata

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.2.3.120 37
-
 assay at Mentha spicata
4.2.3.122 37
-
 assay at Mentha spicata

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.2.3.120 7
-
 assay at Mentha spicata
4.2.3.122 7
-
 assay at Mentha spicata

General Information

EC Number General Information Comment Organism
4.2.3.120 additional information plasticity of the active site Mentha spicata
4.2.3.120 physiological function 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 Mentha spicata
4.2.3.122 additional information plasticity of the active site Mentha spicata
4.2.3.122 physiological function 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 Mentha spicata