KEGG   ENZYME: 4.2.3.127
Entry
EC 4.2.3.127                Enzyme                                 
Name
beta-copaene synthase;
cop4
Class
Lyases;
Carbon-oxygen lyases;
Acting on phosphates
Sysname
(2E,6E)-farnesyl-diphosphate diphosphate-lyase (cyclizing, beta-copaene-forming)
Reaction(IUBMB)
(2E,6E)-farnesyl diphosphate = beta-copaene + diphosphate [RN:R10006]
Reaction(KEGG)
R10006
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
Orthology
K22058  cubebol/beta-copaene/beta-cubebene/(+)-sativene synthase
Genes
CCICC1G_06441
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 72:1181-95 (2009)
DOI:10.1111/j.1365-2958.2009.06717.x
  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 11:1093-106 (2010)
DOI:10.1002/cbic.200900671
  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 76:7723-33 (2010)
DOI:10.1128/AEM.01811-10
Other DBs
ExplorEnz - The Enzyme Database: 4.2.3.127
IUBMB Enzyme Nomenclature: 4.2.3.127
ExPASy - ENZYME nomenclature database: 4.2.3.127
BRENDA, the Enzyme Database: 4.2.3.127

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