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Beta-cubebene synthase

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"Mg25" redirects here. For the isotope of magnesium (Mg-25 or Mg), see Magnesium-25.
β-cubebene synthase
Identifiers
EC no.4.2.3.128
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β-Cubebene synthase (EC 4.2.3.128, cop4, Mg25) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase (cyclizing, β-cubebene-forming). This enzyme catalyses the following chemical reaction

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

Isolated from the fungus Coprinus cinereus.

References

  1. Lee S, Chappell J (July 2008). "Biochemical and genomic characterization of terpene synthases in Magnolia grandiflora". Plant Physiology. 147 (3): 1017–33. doi:10.1104/pp.108.115824. PMC 2442544. PMID 18467455.
  2. 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.
  3. 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.
  4. 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
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Regulation
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