Literature summary for 4.2.3.B66 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 .

Search for more literature for 4.2.3.B66

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

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

Localization

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

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ent-copalyl diphosphate	Ricinus communis	via reaction intermediates ent-pimarenyl and ent-beyeranyl	ent-beyerene + diphosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Ricinus communis	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
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)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ent-copalyl diphosphate	via reaction intermediates ent-pimarenyl and ent-beyeranyl	Ricinus communis	ent-beyerene + 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
KS(-like) enzyme	-	Ricinus communis
KS(L)	-	Ricinus communis
RcKS(L)	-	Ricinus communis
RcKSL4	-	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 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
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