KEGG   ENZYME: 4.2.3.127Help
Entry
EC 4.2.3.127                Enzyme                                 

Name
beta-copaene synthase;
cop4
Class
Lyases;
Carbon-oxygen lyases;
Acting on phosphates
BRITE hierarchy
Sysname
(2E,6E)-farnesyl-diphosphate diphosphate-lyase (cyclizing, beta-copaene-forming)
Reaction(IUBMB)
(2E,6E)-farnesyl diphosphate = beta-copaene + diphosphate [RN:R10006]
Reaction(KEGG)
Substrate
(2E,6E)-farnesyl diphosphate [CPD:C00448]
Product
beta-copaene [CPD:C20274];
diphosphate [CPD:C00013]
Comment
Isolated from the fungus Coprinus cinereus. The enzyme also forms (+)-delta-cadinene, beta-cubebene, (+)-sativene and traces of several other sequiterpenoids [1-3]. beta-Copaene is formed in the presence of Mg2+ but not Mn2+ [2]. See EC 4.2.3.13, (+)-delta-cadinene synthase, EC 4.2.3.128, beta-cubebene synthase, and EC 4.2.3.129, (+)-sativene synthase.
History
EC 4.2.3.127 created 2012
Reference
1  [PMID:19400802]
  Authors
Agger S, Lopez-Gallego F, Schmidt-Dannert C
  Title
Diversity of sesquiterpene synthases in the basidiomycete Coprinus cinereus.
  Journal
Mol. Microbiol. 72 (2009) 1181-95.
  Sequence
Reference
2  [PMID:20419721]
  Authors
Lopez-Gallego F, Agger SA, Abate-Pella D, Distefano MD, Schmidt-Dannert C
  Title
Sesquiterpene synthases Cop4 and Cop6 from Coprinus cinereus: catalytic promiscuity and cyclization of farnesyl pyrophosphate geometric isomers.
  Journal
Chembiochem. 11 (2010) 1093-106.
  Sequence
Reference
3  [PMID:20889795]
  Authors
Lopez-Gallego F, Wawrzyn GT, Schmidt-Dannert C
  Title
Selectivity of fungal sesquiterpene synthases: role of the active site's H-1 alpha loop in catalysis.
  Journal
Appl. Environ. Microbiol. 76 (2010) 7723-33.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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