EC Number   |
General Information |
Reference |
|---|
  4.2.3.44 | evolution |
IrKSL3 and IrKSL6 have the gammabetaalpha tridomain structure, as these proteins tend to possess the bidomain structure of IrKSL1, highlighting the evolutionary history of KSL gene domain loss and further elucidating chemical diversity evolution from a macroevolutionary stance in Lamiaceae. Identified IrCPS4 is predicted to be involved in oridonin biosynthesis, three KSL genes are involved in ent-CPP interactions, and a normal-CPP mediated miltiradiene and isopimaradiene biosynthesis pathway. The three KSL genes bearing different domain structures are involved in the normal-CPP mediated biosynthesis. The tridomain enzymes (IrKSL3 and IrKSL6) belong to an ancestral KSL clade that has the loss of g domain, a widespread occurrence in the Lamiaceae. Evolutionary origin of the gamma-domain loss |
743504 |
| 4.2.3.44 | evolution |
the enzyme belongs to the class I diterpene synthases (DiTPSs). Phylogenetic tree, joining trees of Isodon lophanthoides diTPSs with known class II and class I enzymes based on aligned protein sequences, overview. IlKSL5 belongs to a sub-clade involved in specialized metabolism |
775070 |
| 4.2.3.44 | malfunction |
the Ile and Val mutants with relatively large aliphatic side chains may change the substrate conformation and shield the carbocation of the pimar-15-en-8-yl+ intermediate, thus preventing the addition of a water molecule. By contrast, Ala and other small and/or hydrophilic residues, e.g. Ser and Thr may allow the contact between the pimar-15-en-8-yl+ intermediate and a water molecule, leading to the carbocation neutralization through the addition of a water molecule to form nezukol. In addition, mutation of IrTPS Ala 523 that corresponds to IlKSL5 A513 to Ile shows the same effect by altering product from nezukol to isopimar-7,15-diene |
775070 |
| 4.2.3.44 | metabolism |
a complex repertoire of diterpenoids is found in Artemisia annua with important roles in glandular trichome (GT) formation, artemisinin accumulation and stress resilience. Metabolic engineering of diterpenoids simultaneously increases the artemisinin yield and stress resistance. Transcriptome and metabolic profiling suggests that bioactive gibberellins (GAs) GA4/GA1 promote GT formation. Protein-protein interactions (PPIs) between AaKSL1 and AaCPS2 in the plastids highlighted their potential functions in modulating metabolic flux to gibberellins (GAs) or ent-isopimara-7,15-diene-derived metabolites (IDMs) through metabolic engineering |
774745 |
| 4.2.3.44 | metabolism |
biosynthetic pathway of specialized and general metabolism of diterpenoids in medicinal plant Isodon lophanthoides var. gerardiana, overview. Diverse diTPSs producing distinct diterpene scaffolds form the foundation of the diterpene chemical diversity. Diterpene scaffolds are further modified by P450s and other modification enzymes |
775070 |
| 4.2.3.44 | metabolism |
ent-kaurene diterpenoids are the largest group of known Isodon diterpenoids, five copalyl diphosphate synthase (CPS) and six kaurene synthase-like (KSL) genes are identified by transcriptome profiling of Isodon rubescens leaves. IrKSL6 reacts with normal-CP, synthesized by (+)-copalyl diphosphate synthases IrCPS1 or IrCPS2 (EC 5.5.1.12) to produce isopimaradiene. Enzyme IrKSL2 generates a product with identical EI mass spectrum to isopimaradiene (isopimara-7,15-diene), from ent-copalyl diphosphate |
743504 |
| 4.2.3.44 | metabolism |
the bifunctional diterpene synthase, isopimara-7,15-diene synthase (diTPS-ISO) and a multifunctional cytochrome P450, CYP720B4 perform the biosynthesis of isopimaric acid. The diterpene synthase converts geranylgeranyl diphosphate (GGPP) to the tricyclic diterpene isopimara-7,15-diene (isopimaradiene) via formation of (+)-copalyl diphosphate. In three subsequent oxygenation reactions, the endoplasmic reticulum-associated enzyme CYP720B4 catalyzes the conversion of isopimaradiene into isopimaric acid, pathway overview |
748238 |
| 4.2.3.44 | more |
the hydrophobicity and the size of amino acid 513 play an important role in determining the addition of water by IlKSL5. To identify the amino acid residue controlling the water addition of enzyme IlKSL5, homology-based structure models of IlKSL5 are created using the crystal structure of abietadiene synthase from Abies grandis (PDB ID 3S9V) as template |
775070 |
| 4.2.3.44 | physiological function |
enzymes from diTPS class II and class I, AaCPS2 and AaKSL1, respectively, interact and function in specialized diterpenoid metabolism as a defense against stress. AaKSL1 converts ent-copalyl diphosphate (ent-CPP) into ent-isopimara-7,15-diene. Simultaneous overexpression of AaCPS2 and AaKSL1 may increase gibberellic acid and ent-isopimara-7,15-diene-derived metabolite (IDM) biosynthesis at the same time. Antifungal activity of ent-isopimara-7,15-diene-derived metabolites against Fusarium oxysporum |
774745 |
| 4.2.3.44 | physiological function |
the chloroplastidic bifunctional diterpene synthase, isopimara-7,15-diene synthase (diTPS-ISO) from Picea abies and a cytosolic multifunctional cytochrome P450 (CYP720B4, UniProt ID E5FA70) from Picea sitchensis, which is associated to the endoplasmic reticulum. The diterpene synthase diTPS-ISO also converts geranylgeranyl diphosphate (GGPP) to the tricyclic diterpene isopimara-7,15-diene (isopimaradiene) |
748238 |
