Botryococcene synthase
In this article, we will explore the fascinating world of Botryococcene synthase. From its origin to its influence on modern society, Botryococcene synthase has played a crucial role in various areas of daily life. Throughout history, Botryococcene synthase has been a source of inspiration, contemplation and debate, generating a significant impact on the way people perceive the world around them. Through detailed analysis, we will examine the many facets of Botryococcene synthase, from its roots to its evolution today, providing a complete and enriching insight into this intriguing topic. Join us on this journey of discovery and learning about Botryococcene synthase!
| Botryococcene synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.3.1.97 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Botryococcene synthase (EC 1.3.1.97, SSL-3 (gene)) is an enzyme with systematic name C30 botryococcene:NADP+ oxidoreductase.[1] This enzyme catalyses the following chemical reaction
- C30 botryococcene + NADP+ + diphosphate presqualene diphosphate + NADPH + H+
This enzyme is isolated from the green alga Botryococcus braunii BOT22.
References
- ^ Niehaus TD, Okada S, Devarenne TP, Watt DS, Sviripa V, Chappell J (July 2011). "Identification of unique mechanisms for triterpene biosynthesis in Botryococcus braunii". Proceedings of the National Academy of Sciences of the United States of America. 108 (30): 12260–5. Bibcode:2011PNAS..10812260N. doi:10.1073/pnas.1106222108. PMC 3145686. PMID 21746901.
External links
- Botryococcene+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
