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Literature summary for 4.2.3.19 extracted from

  • Zhan, X.; Bach, S.S.; Hansen, N.L.; Lunde, C.; Simonsen, H.T.
    Additional diterpenes from Physcomitrella patens synthesized by copalyl diphosphate/kaurene synthase (PpCPS/KS) (2015), Plant Physiol. Biochem., 96, 110-114 .
    View publication on PubMed
Search for more literature for 4.2.3.19

Cloned(Commentary)

Cloned (Comment) Organism
gene PHYPA_009773, recombinant expression in Escherichia coli strain C41, transient expression of PpCPSKS with the suppressor of silencing P19 in leafs of 4-weeks-old Nicotiana benthamiana via Agrobacterium tumefaciens strain AGL-1 mediated transformation Physcomitrium patens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ent-copalyl diphosphate Physcomitrium patens
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 ent-beyerene + diphosphate
-
 ?
ent-copalyl diphosphate Physcomitrium patens
-
 ent-kaur-15-ene + diphosphate
-
 ?
ent-copalyl diphosphate Physcomitrium patens
-
 ent-kaur-16-ene + diphosphate
-
 ?
ent-copalyl diphosphate Physcomitrium patens
-
 ent-sandaracopimaradiene + diphosphate
-
 ?
ent-copalyl diphosphate + H2O Physcomitrium patens
-
 16-hydroxy-ent-kaurene + diphosphate
-
 ?
additional information Physcomitrium patens the bifunctional diterpene synthase PpCPS/KS catalyzes both the reactions of ent-copalyl diphosphate synthase, EC 5.5.1.13, and ent-kaurene synthase. Enzyme CPS produces the precursor for several different diterpenes formed by ent-kaurene synthase, i.e. ent-beyerene, ent-sandaracopimaradiene, ent-kaur-15-ene, ent-kaur-16-ene, and 16-hydroxy-ent-kaurene, via three carbocation intermediates, mechanism, overview. PpCPS/KS is a multiproduct enzyme ?
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 ?

Organism

Organism UniProt Comment Textmining
Physcomitrium patens A5A8G0
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ent-copalyl diphosphate
-
 Physcomitrium patens ent-beyerene + diphosphate
-
 ?
ent-copalyl diphosphate
-
 Physcomitrium patens ent-kaur-15-ene + diphosphate
-
 ?
ent-copalyl diphosphate
-
 Physcomitrium patens ent-kaur-16-ene + diphosphate
-
 ?
ent-copalyl diphosphate
-
 Physcomitrium patens ent-sandaracopimaradiene + diphosphate
-
 ?
ent-copalyl diphosphate + H2O
-
 Physcomitrium patens 16-hydroxy-ent-kaurene + diphosphate
-
 ?
additional information the bifunctional diterpene synthase PpCPS/KS catalyzes both the reactions of ent-copalyl diphosphate synthase, EC 5.5.1.13, and ent-kaurene synthase. Enzyme CPS produces the precursor for several different diterpenes formed by ent-kaurene synthase, i.e. ent-beyerene, ent-sandaracopimaradiene, ent-kaur-15-ene, ent-kaur-16-ene, and 16-hydroxy-ent-kaurene, via three carbocation intermediates, mechanism, overview. PpCPS/KS is a multiproduct enzyme Physcomitrium patens ?
-
 ?
additional information the bifunctional diterpene synthase PpCPS/KS catalyzes both the reactions of ent-copalyl diphosphate synthase and ent-kaurene synthase, EC 4.2.3.19 Physcomitrium patens ?
-
 ?

Synonyms

Synonyms Comment Organism
copalyl diphosphate/kaurene synthase
-
 Physcomitrium patens
PpCPS/KS
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 Physcomitrium patens

General Information

General Information Comment Organism
evolution PpCPS/KS is a multiproduct enzyme. It is one of the evolutionary earliest occurring plant diterpene synthases. Thus, PpCPS/KS may have been a multiproduct platform for later evolved diterpene synthases in plants Physcomitrium patens
physiological function copalyl diphosphate/kaurene synthase from the moss Physcomitrella patens (PpCPS/KS) is a bifunctional diterpene synthase and catalyses the formation of at least four diterpenes, including ent-beyerene, ent-sandaracopimaradiene, ent-kaur-16-ene, and 16-hydroxy-ent-kaurene Physcomitrium patens