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Literature summary for 5.5.1.13 extracted from
- Identification of the single amino acid involved in quenching the ent-kauranyl cation by a water molecule in ent-kaurene synthase of Physcomitrella patens (2011), FEBS J., 278, 123-133.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| A710C | no change in reaction product profile compared to wild-type | Physcomitrium patens |
| A710C | site-directed mutagenesis, the mutant shows unaltered activity and reaction product profile compared to the wild-type Jungermannia subulata JsCPS/KS | Physcomitrium patens |
| A710F | mutant converts geranylgeranyl diphosphate to ent-kaurene as the sole product | Physcomitrium patens |
| A710F | site-directed mutagenesis, the mutant protein shows the same enzymic activity as wild-type Jungermannia subulata JsCPS/KS | Physcomitrium patens |
| A710G | no change in reaction product profile compared to wild-type | Physcomitrium patens |
| A710G | site-directed mutagenesis, the mutant shows unaltered activity and reaction product profile compared to the wild-type Jungermannia subulata JsCPS/KS | Physcomitrium patens |
| A710L | the substitution changes the ratio of ent-kaurene and 16alpha-hydroxy-entkaurane produced. The production of ent-kaurene is increased to the same level as that of 16alpha-hydroxyent-kaurane | Physcomitrium patens |
| A710M | mutant converts geranylgeranyl diphosphate to ent-kaurene as the sole product | Physcomitrium patens |
| A710M | site-directed mutagenesis, the mutant protein shows the same enzymic activity as wild-type Jungermannia subulata JsCPS/KS | Physcomitrium patens |
| A710N | no change in reaction product profile compared to wild-type | Physcomitrium patens |
| A710N | site-directed mutagenesis, the mutant shows unaltered activity and reaction product profile compared to the wild-type Jungermannia subulata JsCPS/KS | Physcomitrium patens |
| A710S | no change in reaction product profile compared to wild-type | Physcomitrium patens |
| A710S | site-directed mutagenesis, the mutant shows unaltered activity and reaction product profile compared to the wild-type Jungermannia subulata JsCPS/KS | Physcomitrium patens |
| C717A | site-directed mutagenesis, the mutant protein shows the same enzymic activity as wild-type Jungermannia subulata JsCPS/KS | 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 /Js574-886 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 | Liochlaena subulata |
| additional information | Jungermannia subulata JsCPS/KS peptide fragments are replaced by the corresponding Physcomitrella patens PpCPS/KS region. A PCR-amplified Jungermannia subulata JsCPS/KS DNA fragment corresponding to amino acids 574-746 is replaced by Physcomitrella patens PpCPS/KS amino acids 566-740. Four chimeric cyclases, Physcomitrella patens Pp566/Js574-746/Pp740, Pp566/Js574-721/Pp715, Pp627/Js635-721/Pp715, and Pp666/Js674-721/Pp715, have enzymic activity and produce only ent-kaurene from geranylgeranyl diphosphate, like Jungermannia subulata JsCPS/KS. The chimeric cyclase Pp566/Js574-634/Pp628 shows the same activity as wild-type PpCPS/KS, converting geranylgeranyl diphosphate to both ent-kaurene and 16alpha-hydroxy-ent-kaurane. Overview mutant chimeric constructs and enzymatic activity | Physcomitrium patens |
| additional information | Jungermannia subulata JsCPS/KS peptide fragments are replaced by the corresponding Physcomitrella patens PpCPS/KS region. A PCR-amplified Jungermannia subulata JsCPS/KS DNA fragment corresponding to amino acids 574-746 is replaced by Physcomitrella patens PpCPS/KS amino acids 566-740. Four chimeric cyclases, Physcomitrella patens Pp566/Js574-746/Pp740, Pp566/Js574-721/Pp715, Pp627/Js635-721/Pp715, and Pp666/Js674-721/Pp715, have enzymic activity and produce only ent-kaurene from geranylgeranyl diphosphate, like Jungermannia subulata JsCPS/KS. The chimeric cyclase Pp566/Js574-634/Pp628 shows the same activity as wild-type PpCPS/KS, converting geranylgeranyl diphosphate to both ent-kaurene and 16alpha-hydroxy-ent-kaurane. Overview mutant chimeric constructs and enzymatic activity | Liochlaena subulata |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Liochlaena subulata | the bifunctional ent-kaurene synthase JsCPS/KS catalyzes the cyclization reaction of geranylgeranyl diphosphate to ent-copalyl diphosohate to produce ent-kaurene, but not 16alpha-hydroxy-ent-kaurane | ? | - |
? |  |
| additional information | Physcomitrium patens | the bifunctional ent-kaurene synthase PpCPS/KS produces both entkaurene and 16alpha-hydroxy-ent-kaurane from geranylgeranyl diphosphate via ent-copalyl diphosphate | ? | - |
? | |
Organism
| 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 | - |
| Liochlaena subulata | - |
gene TPS | - |
| Physcomitrium patens | - |
- |
- |
| Physcomitrium patens | - |
bifunctional ent-copalyl diphosphate synthase EC 5.5.1.13, and ent-kaurene synthase, EC 4.2.3.19 | - |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| geranylgeranyl diphosphate = ent-copalyl 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 | |
| geranylgeranyl diphosphate = ent-copalyl 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 | Liochlaena subulata |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| geranylgeranyl diphosphate | - |
Physcomitrium patens | ent-copalyl diphosphate | the bifunctional ent-kaurene synthase produces both entkaurene and 16alpha-hydroxy-ent-kaurane from geranylgeranyl diphosphate via ent-copalyl diphosphate | ? | |
| geranylgeranyl diphosphate | - |
Liochlaena subulata | ent-copalyl diphosphate | the bifunctional ent-kaurene synthase produces both entkaurene and 16alpha-hydroxy-ent-kaurane from geranylgeranyl diphosphate via ent-copalyl diphosphate | ? | |
| additional information | the bifunctional ent-kaurene synthase JsCPS/KS catalyzes the cyclization reaction of geranylgeranyl diphosphate to ent-copalyl diphosohate to produce ent-kaurene, but not 16alpha-hydroxy-ent-kaurane | Liochlaena subulata | ? | - |
? | |
| additional information | the bifunctional ent-kaurene synthase PpCPS/KS produces both entkaurene and 16alpha-hydroxy-ent-kaurane from geranylgeranyl diphosphate via ent-copalyl diphosphate | Physcomitrium patens | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CPS | - |
Physcomitrium patens |
| CPS | - |
Liochlaena subulata |
| CPS/KS | - |
Physcomitrium patens |
| CPS/KS | - |
Liochlaena subulata |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | in flowering plants, ent-kaurene is biosynthesized from geranylgeranyl diphosphate by two distinct cyclases, ent-copalyl diphosphate synthase and ent-kaurene synthase | Liochlaena subulata |
| metabolism | in flowering plants, entkaurene is biosynthesized from geranylgeranyl diphosphate by two distinct cyclases, ent-copalyl diphosphate synthase and ent-kaurene synthase | Physcomitrium patens |
| physiological function | ent-kaurene, a tetracyclic diterpene hydrocarbon, is the biosynthetic intermediate of the plant hormone gibberellin, and is synthesized from geranylgeranyl diphosphate via ent-copalyl diphosphate. The bifunctional ent-kaurene synthase CPS/KS produces both entkaurene and 16alpha-hydroxy-ent-kaurane from geranylgeranyl diphosphate via ent-copalyl diphosphate. Hydrophobicity and size of the side chain residue at the PpCPS/KS amino acid 710 is responsible for quenching the ent-kauranyl cation by the addition of a water molecule | Liochlaena subulata |
| physiological function | the bifunctional ent-kaurene synthase CPS/KS produces both entkaurene and 16alpha-hydroxy-ent-kaurane from geranylgeranyl diphosphate via ent-copalyl diphosphate. Hydrophobicity and size of the side chain residue at the PpCPS/KS amino acid 710 is responsible for quenching the ent-kauranyl cation by the addition of a water molecule | Physcomitrium patens |
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