β-Cubebene synthase (EC 4.2.3.128, cop4, Mg25) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase (cyclizing, β-cubebene-forming).[1][2][3][4] This enzyme catalyses the following chemical reaction
| β-cubebene synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.2.3.128 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Isolated from the fungus Coprinus cinereus.
References
edit- ^ Lee S, Chappell J (July 2008). "Biochemical and genomic characterization of terpene synthases in Magnolia grandiflora". Plant Physiology. 147 (3): 1017–33. doi:10.1104/pp.108.115824. PMC 2442544. PMID 18467455.1017-33&rft.date=2008-07&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2442544#id-name=PMC&rft_id=info:pmid/18467455&rft_id=info:doi/10.1104/pp.108.115824&rft.aulast=Lee&rft.aufirst=S&rft.au=Chappell, J&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2442544&rfr_id=info:sid/en.wikipedia.org:Beta-cubebene synthase" class="Z3988">
- ^ Agger S, Lopez-Gallego F, Schmidt-Dannert C (June 2009). "Diversity of sesquiterpene synthases in the basidiomycete Coprinus cinereus". Molecular Microbiology. 72 (5): 1181–95. doi:10.1111/j.1365-2958.2009.06717.x. PMC 2723806. PMID 19400802.1181-95&rft.date=2009-06&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2723806#id-name=PMC&rft_id=info:pmid/19400802&rft_id=info:doi/10.1111/j.1365-2958.2009.06717.x&rft.aulast=Agger&rft.aufirst=S&rft.au=Lopez-Gallego, F&rft.au=Schmidt-Dannert, C&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2723806&rfr_id=info:sid/en.wikipedia.org:Beta-cubebene synthase" class="Z3988">
- ^ Lopez-Gallego F, Agger SA, Abate-Pella D, Distefano MD, Schmidt-Dannert C (May 2010). "Sesquiterpene synthases Cop4 and Cop6 from Coprinus cinereus: catalytic promiscuity and cyclization of farnesyl pyrophosphate geometric isomers". ChemBioChem. 11 (8): 1093–106. doi:10.1002/cbic.200900671. PMC 2873112. PMID 20419721.1093-106&rft.date=2010-05&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2873112#id-name=PMC&rft_id=info:pmid/20419721&rft_id=info:doi/10.1002/cbic.200900671&rft.aulast=Lopez-Gallego&rft.aufirst=F&rft.au=Agger, SA&rft.au=Abate-Pella, D&rft.au=Distefano, MD&rft.au=Schmidt-Dannert, C&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2873112&rfr_id=info:sid/en.wikipedia.org:Beta-cubebene synthase" class="Z3988">
- ^ López-Gallego F, Wawrzyn GT, Schmidt-Dannert C (December 2010). "Selectivity of fungal sesquiterpene synthases: role of the active site's H-1α loop in catalysis". Applied and Environmental Microbiology. 76 (23): 7723–33. Bibcode:2010ApEnM..76.7723L. doi:10.1128/aem.01811-10. PMC 2988597. PMID 20889795.7723-33&rft.date=2010-12&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2988597#id-name=PMC&rft_id=info:pmid/20889795&rft_id=info:doi/10.1128/aem.01811-10&rft_id=info:bibcode/2010ApEnM..76.7723L&rft.aulast=López-Gallego&rft.aufirst=F&rft.au=Wawrzyn, GT&rft.au=Schmidt-Dannert, C&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2988597&rfr_id=info:sid/en.wikipedia.org:Beta-cubebene synthase" class="Z3988">
External links
edit- Beta-cubebene synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
