Misplaced Pages

Beta-copaene synthase

Article snapshot taken from Wikipedia with creative commons attribution-sharealike license. Give it a read and then ask your questions in the chat. We can research this topic together.
β-copaene synthase
Identifiers
EC no.4.2.3.127
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

β-Copaene synthase (EC 4.2.3.127, cop4) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase (cyclizing, β-copaene-forming). This enzyme catalyses the following chemical reaction

(2E,6E)-farnesyl diphosphate {\displaystyle \rightleftharpoons } β-copaene + diphosphate

This enzyme is isolated from the fungus Coprinus cinereus.

References

  1. 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.
  2. 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.
  3. 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.

External links

Carbon–oxygen lyases (EC 4.2) (primarily dehydratases)
4.2.1: Hydro-Lyases
4.2.2: Acting on polysaccharides
4.2.3: Acting on phosphates
4.2.99: Other
Enzymes
Activity
Regulation
Classification
Kinetics
Types
Portal: Category: