Alpha-longipinene synthase
| α-longipinene synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.2.3.80 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
α-Longipinene synthase (EC 4.2.3.80) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase (α-longipinene-forming).[1][2] This enzyme catalyses the following chemical reaction
- (2E,6E)-farnesyl diphosphate α-longipinene + diphosphate
The enzyme from Norway spruce produces longifolene as the main product.
References[edit]
- ^ Martin DM, Fäldt J, Bohlmann J (August 2004). "Functional characterization of nine Norway Spruce TPS genes and evolution of gymnosperm terpene synthases of the TPS-d subfamily". Plant Physiology. 135 (4): 1908–27. doi:10.1104/pp.104.042028. PMC 520763. PMID 15310829.
- ^ Köpke D, Schröder R, Fischer HM, Gershenzon J, Hilker M, Schmidt A (August 2008). "Does egg deposition by herbivorous pine sawflies affect transcription of sesquiterpene synthases in pine?". Planta. 228 (3): 427–38. doi:10.1007/s00425-008-0747-8. PMC 2459234. PMID 18493792.
External links[edit]
- Alpha-longipinene+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
