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Literature summary extracted from

  • Jackson, A.; Hershey, D.; Chesnut, T.; Xu, M.; Peters, R.
    Biochemical characterization of the castor bean ent-kaurene synthase(-like) family supports quantum chemical view of diterpene cyclization (2014), Phytochemistry, 103, 13 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.3.19 expressed in Escherichia coli Top10 cells Ricinus communis
4.2.3.19 isozyme determination and phylogenetic analysis and tree, sequence comparisons, overview. Synthetic RcKS(L) isozymes are truncated to remove the N-terminal plastid-directing transit peptide sequences, they are individually subcloned into compatible expression vectors and each coexpressed with either the geranylgeranyl phosphate synthase (GGPS), or the GGPS along with a CPS (EC 5.5.1.13) for recombinant expression in Escherichia coli Ricinus communis
4.2.3.29 molecular phylogenetic analysis and tree, sequence comparisons, overview. The predicted RcKSL3 encodes an active enzyme, isozyme determination and phylogenetic analysis and tree, sequence comparisons, the synthetic RcKS(L) isozyme is truncated to remove the N-terminal plastid-directing transit peptide sequences, it is individually subcloned into compatible expression vectors and coexpressed with either the geranylgeranyl phosphate synthase (GGPS), or the GGPS along with a CPS (EC 5.5.1.13) for recombinant expression in Escherichia coli Ricinus communis
4.2.3.229 isozyme determination and phylogenetic analysis and tree, sequence comparisons, overview. Synthetic RcKS(L) isozymes are truncated to remove the N-terminal plastid-directing transit peptide sequences, they are individually subcloned into compatible expression vectors and each coexpressed with either the geranylgeranyl phosphate synthase (GGPS), or the GGPS along with a CPS (EC 5.5.1.13) for recombinant expression in Escherichia coli Ricinus communis

Protein Variants

EC Number Protein Variants Comment Organism
4.2.3.19 A676T site-directed mutagenesis of isozyme RcKSL2, mutation of the catalytically important residue results in 60fold increased product amount composed of essentially the same mix of ent-trachylobane and ent-kaurene as observed for the wild-type enzyme Ricinus communis
4.2.3.29 Q676T site-directed mutagenesis of isozyme RcKSL3, mutation of the residue results in 2fold decrease of the amount of ent-sandaracopimaradiene compared to the wild-type enzyme Ricinus communis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
4.2.3.19 chloroplast
-
 Ricinus communis 9507
-
4.2.3.29 chloroplast
-
 Ricinus communis 9507
-
4.2.3.29 additional information the predicted RcKSL3 aa sequence does appear to have a significantly longer N-terminal transit peptide than the other RcKSL Ricinus communis
-
-
4.2.3.229 chloroplast
-
 Ricinus communis 9507
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.2.3.19 Mg2+ isozyme RcKSL2 contains a significant deviation from the usually well-conserved (N/D)Dxx(S/T)xxxE sequence that serves as a secondary Mg2+ binding motif Ricinus communis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.3.19 ent-copalyl diphosphate Ricinus communis
-
 ent-kaurene + diphosphate
-
 ?
4.2.3.19 ent-copalyl diphosphate Ricinus communis
-
 ent-kaur-ene + diphosphate
-
 ?
4.2.3.19 ent-copalyl diphosphate Ricinus communis
-
 ent-trachylobane + diphosphate
-
 ?
4.2.3.29 ent-copalyl diphosphate Ricinus communis
-
 ent-sandaracopimaradiene + diphosphate
-
 ?
4.2.3.229 ent-copalyl diphosphate Ricinus communis via reaction intermediates ent-pimarenyl and ent-beyeranyl ent-beyerene + diphosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.2.3.19 Ricinus communis B9T625
-
-
4.2.3.19 Ricinus communis B9SIL7
-
-
4.2.3.29 Ricinus communis
-
-
-
4.2.3.229 Ricinus communis
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
4.2.3.19 ent-copalyl diphosphate = ent-kaurene + diphosphate cyclization mechanism derived from quantum chemical calculation for the formation of ent-kaurene and related diterpenes, overview Ricinus communis
a
4.2.3.29 ent-copalyl diphosphate = ent-sandaracopimara-8(14),15-diene + diphosphate reaction via ent-isopimaranyl intermediate Ricinus communis
a
4.2.3.229 ent-copalyl diphosphate = ent-beyerene + diphosphate cyclization mechanism derived from quantum chemical calculation for the formation of ent-kaurene and related diterpenes, overview Ricinus communis
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.3.19 ent-copalyl diphosphate
-
 Ricinus communis ent-kaurene + diphosphate
-
 ?
4.2.3.19 ent-copalyl diphosphate
-
 Ricinus communis ent-kaur-ene + diphosphate
-
 ?
4.2.3.19 ent-copalyl diphosphate
-
 Ricinus communis ent-trachylobane + diphosphate
-
 ?
4.2.3.19 additional information the enzyme forms ent-kaurene via 4 consecutive intermediates (i.e. ent-pimarenyl, ent-beyeranyl, ent-trachylobanyl, and ent-kauranyl), three of which can be the precursor for different diterpenes other than ent-kaurene, overview. Enzyme product analysis by GC-MS. No production of ent-beyerene or ent-atiserene by isozymes RcKSL1 and RcKSL2 Ricinus communis ?
-
 ?
4.2.3.29 ent-copalyl diphosphate
-
 Ricinus communis ent-sandaracopimaradiene + diphosphate
-
 ?
4.2.3.29 ent-copalyl diphosphate isozyme RcKSL3 produces ent-sandaracopimaradiene (94%) along with small amounts of ent-labdatriene (3%) and ent-pimaradiene (3%) Ricinus communis ent-sandaracopimaradiene + diphosphate
-
 ?
4.2.3.29 additional information enzyme product analysis by GC-MS Ricinus communis ?
-
 ?
4.2.3.229 ent-copalyl diphosphate via reaction intermediates ent-pimarenyl and ent-beyeranyl Ricinus communis ent-beyerene + diphosphate
-
 ?
4.2.3.229 additional information the enzyme forms ent-kaurene via 4 consecutive intermediates (i.e. ent-pimarenyl, ent-beyeranyl, ent-trachylobanyl, and ent-kauranyl), three of which can be the precursor for different diterpenes other than ent-kaurene, overview. Enzyme product analysis by GC-MS. No production of ent-beyerene or ent-atiserene by isozymes RcKSL1 and RcKSL2 Ricinus communis ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.2.3.19 ent-kaurene synthase
-
 Ricinus communis
4.2.3.19 ent-kaurene synthase B
-
 Ricinus communis
4.2.3.19 KS(-like) enzyme
-
 Ricinus communis
4.2.3.19 KS(L)
-
 Ricinus communis
4.2.3.19 KSL1
-
 Ricinus communis
4.2.3.19 RcKS(L)
-
 Ricinus communis
4.2.3.19 RcKS1
-
 Ricinus communis
4.2.3.19 RcKSL1
-
 Ricinus communis
4.2.3.19 RcKSL2
-
 Ricinus communis
4.2.3.19 RCOM_0823080
-
 Ricinus communis
4.2.3.29 KS(-like) enzyme
-
 Ricinus communis
4.2.3.29 KS(L)
-
 Ricinus communis
4.2.3.29 RcKS(L)
-
 Ricinus communis
4.2.3.29 RcKSL3
-
 Ricinus communis
4.2.3.229 KS(-like) enzyme
-
 Ricinus communis
4.2.3.229 KS(L)
-
 Ricinus communis
4.2.3.229 RcKS(L)
-
 Ricinus communis
4.2.3.229 RcKSL4
-
 Ricinus communis

General Information

EC Number General Information Comment Organism
4.2.3.19 evolution plants have extensively diversified their arsenal of labdane-related diterpenoids (LRDs), in part via gene duplication and neo-functionalization of the ancestral ent-kaurene synthase (KS) required for gibberellin metabolism. Ricinus communis contains 4 RcKSL isozymes, molecular phylogenetic analysis indicates that RcKSL1 is significantly more closely related to dicotyl ent-kaurene synthases (KSs), while the other three, RcKSL2-4, cluster separately. RcKSL2-4 are in close proximity to each other, within a region of 65 kb, with RcKSL2 and 4 occurring as a tandem gene pair. RcKSL1 is the only isozyme to react with ent-CPP producing small amounts of ent-kaurene, and is referred to as RcKS1. Both RcKSL2 and RcKSL3 also are selectively reacting with ent-CPP with RcKSL2 producing primarily ent-trachylobane (70%) as well as smaller amounts of ent-kaurene (30%), and RcKSL3 producing ent-sandaracopimaradiene (94%) (EC 4.2.3.29) along with small amounts of ent-labdatriene (3%) and ent-pimaradiene (3%). RcKSL4 seems to be inactive, with no products evident from any substrate, but upon synthesis of a codon-optimized gene for the corrected aa sequence and functional analysis, RcKSL4 selectively reacts with ent-CPP and produces largely ent-beyerene (95%) along with very small amounts of ent-atiserene (4%) and ent-kaurene (1%). The enzymes belong to the terpene synthase family Ricinus communis
4.2.3.19 physiological function plants have extensively diversified their arsenal of labdane-related diterpenoids (LRDs), in part via gene duplication and neo-functionalization of the ancestral ent-kaurene synthase (KS) required for gibberellin metabolism Ricinus communis
4.2.3.29 evolution plants have extensively diversified their arsenal of labdane-related diterpenoids (LRDs), in part via gene duplication and neo-functionalization of the ancestral ent-kaurene synthase (KS) required for gibberellin metabolism. Ricinus communis contains 4 RcKSL isozymes, molecular phylogenetic analysis indicates that RcKS(L)1 is significantly more closely related to dicotyl ent-kaurene synthases (KSs), while the other three, RcKSL2-4, cluster separately. RcKSL2-4 are in close proximity to each other, within a region of 65 kb, with RcKSL2 and 4 occurring as a tandem gene pair. RcKS(L)1 is the only isozyme to react with ent-CPP producing small amounts of ent-kaurene, and is referred to as RcKS1. Both RcKSL2 and RcKSL3 also are selectively reacting with ent-CPP with RcKSL2 producing primarily ent-trachylobane (70%) as well as smaller amounts of ent-kaurene (30%), and RcKSL3 producing ent-sandaracopimaradiene (94%) (EC 4.2.3.29) along with small amounts of ent-labdatriene (3%) and ent-pimaradiene (3%). RcKSL4 seems to be inactive, with no products evident from any substrate, but upon synthesis of a codon-optimized gene for the corrected aa sequence and functional analysis, RcKSL4 selectively reacts with ent-CPP and produces largely ent-beyerene (95%) along with very small amounts of ent-atiserene (4%) and ent-kaurene (1%). The enzymes belong to the terpene synthase family and is a class I diterpene synthase Ricinus communis
4.2.3.229 evolution plants have extensively diversified their arsenal of labdane-related diterpenoids (LRDs), in part via gene duplication and neo-functionalization of the ancestral ent-kaurene synthase (KS) required for gibberellin metabolism. Ricinus communis contains 4 RcKSL isozymes, molecular phylogenetic analysis indicates that RcKS(L)1 is significantly more closely related to dicotyl ent-kaurene synthases (KSs), while the other three, RcKSL2-4, cluster separately. RcKSL2-4 are in close proximity to each other, within a region of 65 kb, with RcKSL2 and 4 occurring as a tandem gene pair. RcKS(L)1 is the only isozyme to react with ent-CPP producing small amounts of ent-kaurene, and is referred to as RcKS1. Both RcKSL2 and RcKSL3 also are selectively reacting with ent-CPP with RcKSL2 producing primarily ent-trachylobane (70%) as well as smaller amounts of ent-kaurene (30%), and RcKSL3 producing ent-sandaracopimaradiene (94%) (EC 4.2.3.29) along with small amounts of ent-labdatriene (3%) and ent-pimaradiene (3%). RcKSL4 seems to be inactive, with no products evident from any substrate, but upon synthesis of a codon-optimized gene for the corrected aa sequence and functional analysis, RcKSL4 selectively reacts with ent-CPP and produces largely ent-beyerene (95%) along with very small amounts of ent-atiserene (4%) and ent-kaurene (1%). The enzymes belong to the terpene synthase family Ricinus communis
4.2.3.229 physiological function plants have extensively diversified their arsenal of labdane-related diterpenoids (LRDs), in part via gene duplication and neo-functionalization of the ancestral ent-kaurene synthase (KS) required for gibberellin metabolism Ricinus communis