KEGG   ENZYME: 4.2.3.129Help
Entry
EC 4.2.3.129                Enzyme                                 

Name
(+)-sativene synthase;
cop4
Class
Lyases;
Carbon-oxygen lyases;
Acting on phosphates
BRITE hierarchy
Sysname
(2E,6E)-farnesyl-diphosphate diphosphate-lyase (cyclizing, (+)-sativene-forming)
Reaction(IUBMB)
(2E,6E)-farnesyl diphosphate = (+)-sativene + diphosphate [RN:R10008]
Reaction(KEGG)
Substrate
(2E,6E)-farnesyl diphosphate [CPD:C00448]
Product
(+)-sativene [CPD:C20275];
diphosphate [CPD:C00013]
Comment
Isolated from the fungus Coprinus cinereus. The enzyme also forms (+)-delta-cadinene, beta-copaene, beta-cubebene, and traces of several other sequiterpenoids. See EC 4.2.3.13, (+)-delta-cadinene synthase, EC 4.2.3.127, beta-copaene synthase, and EC 4.2.3.128, beta-cubebene synthase.
History
EC 4.2.3.129 created 2012
Orthology
K22058  cubebol/beta-copaene/beta-cubebene/(+)-sativene synthase
Genes
CCI: CC1G_06441
Taxonomy
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
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 4.2.3.129
IUBMB Enzyme Nomenclature: 4.2.3.129
ExPASy - ENZYME nomenclature database: 4.2.3.129
BRENDA, the Enzyme Database: 4.2.3.129

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