| RRC ID |
1892
|
| 著者 |
Hayashi K, Kawaide H, Notomi M, Sakigi Y, Matsuo A, Nozaki H.
|
| タイトル |
Identification and functional analysis of bifunctional ent-kaurene synthase from the moss Physcomitrella patens.
|
| ジャーナル |
FEBS Lett
|
| Abstract |
ent-Kaurene is the key intermediate in biosynthesis of gibberellins (GAs), plant hormones. In higher plants, ent-kaurene is synthesized successively by copalyl diphosphate synthase (CPS) and ent-kaurene synthase (KS) from geranylgeranyl diphosphate (GGDP). On the other hand, fungal ent-kaurene synthases are bifunctional cyclases with both CPS and KS activity in a single polypeptide. The moss Physcomitrella patens is a model organism for the study of genetics and development in an early land plant. We identified ent-kaurene synthase (PpCPS/KS) from P. patens and analyzed its function. PpCPS/KS cDNA encodes a 101-kDa polypeptide, and shows high similarity with CPSs and abietadiene synthase from higher plants. PpCPS/KS is a bifunctional cyclase and, like fungal CPS/KS, directly synthesizes the ent-kaurene skeleton from GGDP. PpCPS/KS has two aspartate-rich DVDD and DDYFD motifs observed in CPS and KS, respectively. The mutational analysis of two conserved motifs in PpCPS/KS indicated that the DVDD motif is responsible for CPS activity (GGDP to CDP) and the DDYFD motif for KS activity (CDP to ent-kaurene and ent-16alpha-hydroxykaurene).
|
| 巻・号 |
580(26)
|
| ページ |
6175-81
|
| 公開日 |
2006-11-13
|
| DOI |
10.1016/j.febslet.2006.10.018
|
| PII |
S0014-5793(06)01224-5
|
| PMID |
17064690
|
| MeSH |
Alkyl and Aryl Transferases / genetics*
Alkyl and Aryl Transferases / physiology*
Amino Acid Motifs
Amino Acid Sequence
Bryophyta / enzymology*
Mutagenesis, Site-Directed
Phylogeny
Plant Proteins
Sequence Alignment
|
| IF |
3.057
|
| 引用数 |
119
|
|
WOS 分野
|
BIOPHYSICS
BIOCHEMISTRY & MOLECULAR BIOLOGY
CELL BIOLOGY
|
| リソース情報 |
| シロイヌナズナ / 植物培養細胞・遺伝子 |
pdp33101 |
