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Literature summary for 4.2.3.19 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)

Cloned (Comment) Organism
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

Protein Variants Comment Organism
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

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast
-
Ricinus communis 9507
-

Metals/Ions

Metals/Ions Comment Organism Structure
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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ent-copalyl diphosphate Ricinus communis
-
ent-kaur-ene + diphosphate
-
?
ent-copalyl diphosphate Ricinus communis
-
ent-trachylobane + diphosphate
-
?

Organism

Organism UniProt Comment Textmining
Ricinus communis B9SIL7
-
-

Reaction

Reaction Comment Organism Reaction ID
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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ent-copalyl diphosphate
-
Ricinus communis ent-kaurene + diphosphate
-
?
ent-copalyl diphosphate
-
Ricinus communis ent-kaur-ene + diphosphate
-
?
ent-copalyl diphosphate
-
Ricinus communis ent-trachylobane + diphosphate
-
?
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

Synonyms Comment Organism
ent-kaurene synthase B
-
Ricinus communis
KS(-like) enzyme
-
Ricinus communis
KS(L)
-
Ricinus communis
RcKS(L)
-
Ricinus communis
RcKS1
-
Ricinus communis
RcKSL1
-
Ricinus communis
RcKSL2
-
Ricinus communis
RCOM_0823080
-
Ricinus communis

General Information

General Information Comment Organism
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
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