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Literature summary for 4.2.3.131 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)

Cloned (Comment) Organism
expressed in Saccharomyces cerevisiae Salvia miltiorrhiza

Protein Variants

Protein Variants Comment Organism
D391G/D392G the mutant converts only (+)-copalyl diphosphate but not ent- or syn-copalyl diphosphate Salvia miltiorrhiza
D611G/D612G the mutant converts geranylgeranyl diphosphate to ent-copalyl diphosphate Salvia miltiorrhiza

Organism

Organism UniProt Comment Textmining
Salvia miltiorrhiza
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(+)-copalyl diphosphate
-
Salvia miltiorrhiza miltiradiene + diphosphate
-
?
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 ?
-
?

Synonyms

Synonyms Comment Organism
kaurene synthase-like
-
Salvia miltiorrhiza
KSL
-
Salvia miltiorrhiza