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Literature summary extracted from

  • Sugai, Y.; Ueno, Y.; Hayashi, K.; Oogami, S.; Toyomasu, T.; Matsumoto, S.; Natsume, M.; Nozaki, H.; Kawaide, H.
    Enzymatic (13)C labeling and multidimensional NMR analysis of miltiradiene synthesized by bifunctional diterpene cyclase in Selaginella moellendorffii (2011), J. Biol. Chem., 286, 42840-42847.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.3.131 expressed in Saccharomyces cerevisiae Salvia miltiorrhiza

Protein Variants

EC Number Protein Variants Comment Organism
4.2.3.131 D391G/D392G the mutant converts only (+)-copalyl diphosphate but not ent- or syn-copalyl diphosphate Salvia miltiorrhiza
4.2.3.131 D611G/D612G the mutant converts geranylgeranyl diphosphate to ent-copalyl diphosphate Salvia miltiorrhiza
5.5.1.12 D391G/D392G site-directed mutagenesis of DIDD motif residues, the mutant lacks type-B activity Selaginella moellendorffii
5.5.1.12 D611G/D612G site-directed mutagenesis of DDLMD motif residues, the mutant lacks type-A cyclase activity Selaginella moellendorffii

Organism

EC Number Organism UniProt Comment Textmining
4.2.3.131 Salvia miltiorrhiza
-
-
-
5.5.1.12 Selaginella moellendorffii G9MAN7
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.3.131 (+)-copalyl diphosphate
-
Salvia miltiorrhiza miltiradiene + diphosphate
-
?
4.2.3.131 additional information MDS is a bifunctional miltiradiene synthase catalyzing the cyclization reaction of geranylgeranyl diphosphate via (+)-copalyl diphosphate to afford miltiradiene as a final product Salvia miltiorrhiza ?
-
?
5.5.1.12 geranylgeranyl diphosphate BDTC-like enzyme, miltiradiene synthase converts geranylgeranyl diphosphate to a diterpene hydrocarbon product with a molecular mass of 272 Da. Mutation in the type-B active motif of BDTC-like enzyme miltiradiene synthase, D611G/D612G, abolishes the cyclase activity, whereas (+)-copalyl diphosphate, the reaction intermediate from the conversion of geranylgeranyl diphosphate to the hydrocarbon product, rescues the cyclase activity of the mutant to form a diterpene hydrocarbon. Another mutant lacking type-A activity, D391G/D392G, accumulates copalyl diphosphate as the reaction intermediate Selaginella moellendorffii (+)-copalyl diphosphate
-
?
5.5.1.12 additional information miltiradiene synthesis reaction with geranylgeranyl diphosphate to miltiradiene, EC 4.2.3.131, via (+)-copalyl diphosphate intermediate, not ent-copalyl diphosphate. The enzyme catalyzes the successive two-step type-B (protonation-initiated cyclization) and type-A (ionization-initiated cyclization) reactions of geranylgeranyl diphosphate. The two aspartate-rich motifs, 389DIDD and 611DDLMD, that are required for the type-B and type-A cyclization reactions, respectively. Product analysis by GC-MS and NMR spectroscopy Selaginella moellendorffii ?
-
?

Synonyms

EC Number Synonyms Comment Organism
4.2.3.131 kaurene synthase-like
-
Salvia miltiorrhiza
4.2.3.131 KSL
-
Salvia miltiorrhiza
5.5.1.12 BDTC
-
Selaginella moellendorffii
5.5.1.12 bifunctional diterpene cyclase
-
Selaginella moellendorffii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
5.5.1.12 28
-
assay at Selaginella moellendorffii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5.1.12 7.5
-
assay at Selaginella moellendorffii

General Information

EC Number General Information Comment Organism
5.5.1.12 metabolism bifunctional diterpene cyclases are involved in hormone and defense compound biosyntheses in bryophytes and gymnosperms, respectively Selaginella moellendorffii
5.5.1.12 additional information enzyme structure by two-dimensional and three-dimensional NMR Selaginella moellendorffii