Protein Variants | Comment | Organism |
---|---|---|
A710C | no change in reaction product profile compared to wild-type | Physcomitrium patens |
A710F | mutant converts geranylgeranyl diphosphate to ent-kaurene as the sole product | Physcomitrium patens |
A710G | no change in reaction product profile compared to wild-type | Physcomitrium patens |
A710M | mutant converted geranylgeranyl diphosphate to ent-kaurene as the sole product | Physcomitrium patens |
A710N | no change in reaction product profile compared to wild-type | Physcomitrium patens |
A710S | no change in reaction product profile compared to wild-type | Physcomitrium patens |
additional information | construction of chimeric proteins of Physcomitrella patens PpCPS/KS with Jungermannia subulata, the chimeric cyclases Pp131-566 /Js574-886 and Pp131-504 /Js512-886 and produce only ent-kaurene. Chimeric cyclases, Pp131-622 /Js630-886 and Pp131-714 /Js722-886, lose all enzymic activity | Physcomitrium patens |
additional information | construction of chimeric proteins of Physcomitrella patens PpCPS/KS with Jungermannia subulata, the chimeric cyclases Pp131-566 /Js574-86 and Pp131-504 /Js512-886 and produce only ent-kaurene. Chimeric cyclases, Pp131-622 /Js630-886 and Pp131-714 /Js722-886, lose all enzymic activity | Liochlaena subulata |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Liochlaena subulata | - |
bifunctional ent-copalyl diphosphate synthase EC 5.5.1.13, and ent-kaurene synthase, EC 4.2.3.19 | - |
Physcomitrium patens | A5A8G0 | bifunctional ent-copalyl diphosphate synthase EC 5.5.1.13, and ent-kaurene synthase, EC 4.2.3.19 | - |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
ent-copalyl diphosphate = ent-kaurene + diphosphate | the determination of the final products of CPS/KSs in bryophytes depends on the sequence and structure of the C-terminal regions of CPS/KSs. Thus, the type A cyclization reaction of both PpCPS/KS and JsCPS /KS occurs near the C-terminal region of the polypeptides | Liochlaena subulata | |
ent-copalyl diphosphate = ent-kaurene + diphosphate | the hydrophobicity and size of the side chain residue at the bifunctional CPS/KS amino acid 710 is responsible for quenching the ent-kauranyl cation by the addition of a water molecule. The determination of the final products of CPS/KSs in bryophytes depends on the sequence and structure of the C-terminal regions of CPS/KSs. Thus, the type A cyclization reaction of both PpCPS/KS and JsCPS /KS occurs near the C-terminal region of the polypeptides | Physcomitrium patens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ent-copalyl diphosphate | - |
Physcomitrium patens | ent-kaurene + diphosphate | the bifunctional ent-kaurene synthase produces both entkaurene and 16alpha-hydroxy-ent-kaurane from geranylgeranyl diphosphate via ent-copalyl diphosphate | ? | |
ent-copalyl diphosphate | - |
Liochlaena subulata | ent-kaurene + diphosphate | the bifunctional ent-kaurene synthase produces both entkaurene and 16alpha-hydroxy-ent-kaurane from geranylgeranyl diphosphate via ent-copalyl diphosphate | ? | |
ent-copalyl diphosphate + H2O | - |
Physcomitrium patens | 16alpha-hydroxy-ent-kaurane + diphosphate | the bifunctional ent-kaurene synthase produces both entkaurene and 16alpha-hydroxy-ent-kaurane from geranylgeranyl diphosphate via ent-copalyl diphosphate | ? | |
ent-copalyl diphosphate + H2O | - |
Liochlaena subulata | 16alpha-hydroxy-ent-kaurane + diphosphate | the bifunctional ent-kaurene synthase produces both entkaurene and 16alpha-hydroxy-ent-kaurane from geranylgeranyl diphosphate via ent-copalyl diphosphate | ? |
Synonyms | Comment | Organism |
---|---|---|
CPS/KS | - |
Physcomitrium patens |
CPS/KS | - |
Liochlaena subulata |