Aphidicolan-16beta-ol synthase
| Aphidicolan-16beta-ol synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 4.2.3.42 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Aphidicolan-16beta-ol synthase (EC 4.2.3.42, PbACS) is an enzyme with systematic name 9alpha-copalyl-diphosphate diphosphate-lyase (aphidicolan-16beta-ol-forming).[1][2] This enzyme catalyses the following chemical reaction
- 9alpha-copalyl diphosphate + H2O aphidicolan-16beta-ol + diphosphate
This is a bifunctional enzyme, which also has EC 5.5.1.14 activity.
References
- ↑ Oikawa, H.; Toyomasu, T.; Toshima, H.; Ohashi, S.; Kawaide, H.; Kamiya, Y.; Ohtsuka, M.; Shinoda, S.; Mitsuhashi, W.; Sassa, T. (2001). "Cloning and functional expression of cDNA encoding aphidicolan-16 β-ol synthase: a key enzyme responsible for formation of an unusual diterpene skeleton in biosynthesis of aphidicolin". J. Am. Chem. Soc. 123: 5154–5155. doi:10.1021/ja015747j. PMID 11457369.
- ↑ Toyomasu, T.; Nakaminami, K.; Toshima, H.; Mie, T.; Watanabe, K.; Ito, H.; Matsui, H.; Mitsuhashi, W.; Sassa, T.; Oikawa, H. (2004). "Cloning of a gene cluster responsible for the biosynthesis of diterpene aphidicolin, a specific inhibitor of DNA polymerase α". Biosci. Biotechnol. Biochem. 68: 146–152. doi:10.1271/bbb.68.146. PMID 14745177.
External links
- Aphidicolan-16beta-ol+synthase at the US National Library of Medicine Medical Subject Headings (MeSH)
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