EC 4.2.3.128 - β-cubebene synthase

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IntEnz Enzyme Nomenclature
EC 4.2.3.128

Names

Accepted name:
β-cubebene synthase
Other names:
Cop4
Mg25
Systematic name:
(2E,6E)-farnesyl-diphosphate diphosphate-lyase (cyclizing, β-cubebene-forming)

Reaction

Comments:

Isolated from the fungus Coprinus cinereus. The enzyme also forms (+)-δ-cadinene, β-copaene, (+)-sativene and traces of several other sequiterpenoids [2-4]. It is found in many higher plants such as Magnolia grandiflora (Southern Magnolia) together with germacrene A [1]. See EC 4.2.3.13, (+)-δ-cadinene synthase, EC 4.2.3.127, β-copaene synthase, EC 4.2.3.129, (+)-sativene synthase, and EC 4.2.3.23, germacrene A synthase.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

References

  1. Lee, S., Chappell, J.
    Biochemical and genomic characterization of terpene synthases in Magnolia grandiflora.
    Plant Physiol. 147: 1017-1033 (2008). [PMID: 18467455]
  2. Agger, S., Lopez-Gallego, F., Schmidt-Dannert, C.
    Diversity of sesquiterpene synthases in the basidiomycete Coprinus cinereus.
    Mol. Microbiol. 72: 1181-1195 (2009). [PMID: 19400802]
  3. Lopez-Gallego, F., Agger, S. A., Abate-Pella, D., Distefano, M. D., Schmidt-Dannert, C.
    Sesquiterpene synthases Cop4 and Cop6 from Coprinus cinereus: catalytic promiscuity and cyclization of farnesyl pyrophosphate geometric isomers.
    Chembiochem 11: 1093-1106 (2010). [PMID: 20419721]
  4. Lopez-Gallego, F., Wawrzyn, G. T., Schmidt-Dannert, C.
    Selectivity of fungal sesquiterpene synthases: role of the active site's H-1 alpha loop in catalysis.
    Appl. Environ. Microbiol. 76: 7723-7733 (2010). [PMID: 20889795]

[EC 4.2.3.128 created 2012]