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 | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | 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 | 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 | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Physcomitrium patens | A5A8G0 | - |
- |
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 | Comment | Organism |
---|---|---|
copalyl diphosphate/kaurene synthase | - |
Physcomitrium patens |
PpCPS/KS | - |
Physcomitrium patens |
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 |