EC Number   |
General Information |
Reference |
|---|
    4.2.3.103 | evolution |
enzymes KSLs belong to the type A/class I terpene synthase family. The KSL5 members are clearly divided into two clades, representing japonica and indica groups. The KS responsible for gibberellin biosynthesis in a putative common ancestor, and OsKS1, which produces the tetracyclic ent-kaurene, has Ile as the corresponding key amino acid. Thus, it is suggested that substitution from Ile664 to Thr664 in KSL5 occurred before the onset of cultivation in the putative japonica ancestor. The OsKSL5 sequence is similar to the OsKSL6 sequence (89% identity), and it is therefore likely that the two KSL genes were generated through relatively recent duplication. The substitution in KSL5 probably occurred after duplication of the ancestral gene |
746981 |
| 4.2.3.103 | evolution |
in the plant kingdom, where the labdane-related diterpenoids (LRDs) are predominantly found, the class I and II diterpene cyclases seem to have most directly evolved via gene duplication and neofunctionalization of the ent-kaurene synthases (KSs) required in all vascular plants for gibberellin hormone biosynthesis. Accordingly, these enzymes are often termed KS-like (KSL) and form a distinct subfamily within the plant terpene synthase family. Like class I terpene synthases more generally, the KS(L)s carry out catalysis in a highly conserved alpha-helical bundle domain that contains two signature motifs. These DDxxD and NDxx(S/T)xxxE sequences are involved in ligation of a trinuclear Mg2+ cluster to promote substrate binding and the subsequent initiating ionization of the allylic diphosphate ester bond |
746596 |
| 4.2.3.103 | evolution |
in the plant kingdom, where the labdane-related diterpenoids (LRDs) are predominantly found, the class I and II diterpene cyclases seem to have most directly evolved via gene duplication and neofunctionalization of the ent-kaurene synthases (KSs) required in all vascular plants for gibberellin hormone biosynthesis. Accordingly, these enzymes are often termed KS-like (KSL) and form a distinct subfamily within the plant terpene synthase family. Like class I terpene synthases more generally, the KS(L)s carry out catalysis in a highly conserved alpha-helical bundle domain that contains two signature motifs. These DDxxD and NDxx(S/T)xxxE sequences are involved in ligation of a trinuclear Mg2+ cluster to promote substrate binding and the subsequent initiating ionization of the allylic diphosphate ester bond. OsKSL5 belongs to an early diverging KSL lineage within monocots and is relatively distantly related to any KSs |
746596 |
| 4.2.3.103 | more |
conserved residues at positions 661 (secondary) and 664 (primary) are responsible for substrate specificity. Two functionally distinct alleles of Oryza sativa OsKSL5, which react with ent-copalyl diphosphate (ent-copalyl diphosphate), with that from subspecies japonica (OsKSL5j, EC 4.2.3.30) producing ent-pimara-8(14),15-diene and that from subspecies indica (OsKSL5i, EC 4.2.3.103) producing ent-(iso)kaur-15-ene instead |
746596 |
| 4.2.3.103 | physiological function |
OsKSL5i and OsKSL6, encoding ent-isokaurene synthase, are not responsible for phytocassane biosynthesis, but are suggested to be involved in other specialized diterpenoid metabolism including the synthesis of oryzadiones |
746981 |
| 4.2.3.103 | physiological function |
OsKSL5i and OsKSL6, encoding ent-isokaurene synthase, are not responsible for phytocassane biosynthesis, but are suggested to be involved in other specialized diterpenoid metabolism including the synthesis of oryzadiones. The KSL5 members are clearly divided into two clades, representing japonica and indica groups, the 664th amino acids of OsKSL5j and OsKSL5i are Thr and Ile leading to different activity and production of ent-isokeurene synthase (EC 4.2.3.103) or ent-pimara-8(14),15-diene (EC 4.2.3.30) |
746981 |
| 4.2.3.103 | physiological function |
OsKSL5ind and OsKSL6, encoding ent-isokaurene synthase, are not responsible for phytocassane biosynthesis, but are suggested to be involved in other specialized diterpenoid metabolism including the synthesis of oryzadiones. Recombinant OrKSL5 converts ent-copalyl diphosphate to ent-pimara-8(14),15-diene (cf. EC 4.2.3.30), whereas OrKSL5ind, OrKSL6 and OrKSL6ind all convert ent-copalyl diphosphate to ent-isokaurene. The 664th amino acids of OrKSL5 and OrKSL5ind are Thr and Ile, respectively |
746981 |
| 4.2.3.103 | physiological function |
recombinant OrKSL5 converts ent-copalyl diphosphate to ent-pimara-8(14),15-diene (cf. EC 4.2.3.30), whereas OrKSL5ind, OrKSL6 and OrKSL6ind all convert ent-copalyl diphosphate to ent-isokaurene |
746981 |
| 4.2.3.103 | physiological function |
recombinant OrKSL5 converts ent-copalyl diphosphate to ent-pimara-8(14),15-diene (cf. EC 4.2.3.30), whereas OrKSL5ind, OrKSL6 and OrKSL6ind all convert ent-copalyl diphosphate to ent-isokaurene. The 664th amino acids of OrKSL5 and OrKSL5ind are Thr and Ile, respectively |
746981 |
