Beta-farnesene synthase

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β-farnesene synthase
β-farnesene synthase
Identifiers
EC no.	4.2.3.47
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
PMC
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PMC	articles
PubMed	articles
NCBI	proteins

β-Farnesene synthase (EC 4.2.3.47, farnesene synthase, terpene synthase 10, terpene synthase 10-B73, TPS10) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase ((E)-β-farnesene-forming).^[1]^[2]^[3]^[4]^[5]^[6]^[7]^[8] This enzyme catalyses the following chemical reaction

(2E,6E)-farnesyl diphosphate

\rightleftharpoons

(E)-β-farnesene + diphosphate

References

^ Zhao B, Lei L, Vassylyev DG, Lin X, Cane DE, Kelly SL, Yuan H, Lamb DC, Waterman MR (December 2009). "Crystal structure of albaflavenone monooxygenase containing a moonlighting terpene synthase active site". The Journal of Biological Chemistry. 284 (52): 36711–9. doi:10.1074/jbc.M109.064683. PMC 2794785. PMID 19858213.
^ Picaud S, Brodelius M, Brodelius PE (May 2005). "Expression, purification and characterization of recombinant (E)-β-farnesene synthase from Artemisia annua". Phytochemistry. 66 (9): 961–7. doi:10.1016/j.phytochem.2005.03.027. PMID 15896363.
^ Köllner TG, Gershenzon J, Degenhardt J (June 2009). "Molecular and biochemical evolution of maize terpene synthase 10, an enzyme of indirect defense". Phytochemistry. 70 (9): 1139–45. doi:10.1016/j.phytochem.2009.06.011. PMID 19646721.
^ Schnee C, Köllner TG, Held M, Turlings TC, Gershenzon J, Degenhardt J (January 2006). "The products of a single maize sesquiterpene synthase form a volatile defense signal that attracts natural enemies of maize herbivores". Proceedings of the National Academy of Sciences of the United States of America. 103 (4): 1129–34. Bibcode:2006PNAS..103.1129S. doi:10.1073/pnas.0508027103. PMC 1347987. PMID 16418295.
^ Maruyama T, Ito M, Honda G (October 2001). "Molecular cloning, functional expression and characterization of (E)-beta farnesene synthase from Citrus junos". Biological & Pharmaceutical Bulletin. 24 (10): 1171–5. doi:10.1248/bpb.24.1171. PMID 11642326.
^ Crock J, Wildung M, Croteau R (November 1997). "Isolation and bacterial expression of a sesquiterpene synthase cDNA clone from peppermint (Mentha x piperita, L.) that produces the aphid alarm pheromone (E)-beta-farnesene". Proceedings of the National Academy of Sciences of the United States of America. 94 (24): 12833–8. Bibcode:1997PNAS...9412833C. doi:10.1073/pnas.94.24.12833. PMC 24224. PMID 9371761.
^ Schnee C, Köllner TG, Gershenzon J, Degenhardt J (December 2002). "The maize gene terpene synthase 1 encodes a sesquiterpene synthase catalyzing the formation of (E)-beta-farnesene, (E)-nerolidol, and (E,E)-farnesol after herbivore damage". Plant Physiology. 130 (4): 2049–60. doi:10.1104/pp.008326. PMC 166716. PMID 12481088.
^ Huber DP, Philippe RN, Godard KA, Sturrock RN, Bohlmann J (June 2005). "Characterization of four terpene synthase cDNAs from methyl jasmonate-induced Douglas-fir, Pseudotsuga menziesii". Phytochemistry. 66 (12): 1427–39. doi:10.1016/j.phytochem.2005.04.030. PMID 15921711.

External links

Beta-farnesene+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

[1] Zhao B, Lei L, Vassylyev DG, Lin X, Cane DE, Kelly SL, Yuan H, Lamb DC, Waterman MR (December 2009). "Crystal structure of albaflavenone monooxygenase containing a moonlighting terpene synthase active site". The Journal of Biological Chemistry. 284 (52): 36711–9. doi:10.1074/jbc.M109.064683. PMC 2794785. PMID 19858213.

[2] Picaud S, Brodelius M, Brodelius PE (May 2005). "Expression, purification and characterization of recombinant (E)-β-farnesene synthase from Artemisia annua". Phytochemistry. 66 (9): 961–7. doi:10.1016/j.phytochem.2005.03.027. PMID 15896363.

[3] Köllner TG, Gershenzon J, Degenhardt J (June 2009). "Molecular and biochemical evolution of maize terpene synthase 10, an enzyme of indirect defense". Phytochemistry. 70 (9): 1139–45. doi:10.1016/j.phytochem.2009.06.011. PMID 19646721.

[4] Schnee C, Köllner TG, Held M, Turlings TC, Gershenzon J, Degenhardt J (January 2006). "The products of a single maize sesquiterpene synthase form a volatile defense signal that attracts natural enemies of maize herbivores". Proceedings of the National Academy of Sciences of the United States of America. 103 (4): 1129–34. Bibcode:2006PNAS..103.1129S. doi:10.1073/pnas.0508027103. PMC 1347987. PMID 16418295.

[5] Maruyama T, Ito M, Honda G (October 2001). "Molecular cloning, functional expression and characterization of (E)-beta farnesene synthase from Citrus junos". Biological & Pharmaceutical Bulletin. 24 (10): 1171–5. doi:10.1248/bpb.24.1171. PMID 11642326.

[6] Crock J, Wildung M, Croteau R (November 1997). "Isolation and bacterial expression of a sesquiterpene synthase cDNA clone from peppermint (Mentha x piperita, L.) that produces the aphid alarm pheromone (E)-beta-farnesene". Proceedings of the National Academy of Sciences of the United States of America. 94 (24): 12833–8. Bibcode:1997PNAS...9412833C. doi:10.1073/pnas.94.24.12833. PMC 24224. PMID 9371761.

[7] Schnee C, Köllner TG, Gershenzon J, Degenhardt J (December 2002). "The maize gene terpene synthase 1 encodes a sesquiterpene synthase catalyzing the formation of (E)-beta-farnesene, (E)-nerolidol, and (E,E)-farnesol after herbivore damage". Plant Physiology. 130 (4): 2049–60. doi:10.1104/pp.008326. PMC 166716. PMID 12481088.

[8] Huber DP, Philippe RN, Godard KA, Sturrock RN, Bohlmann J (June 2005). "Characterization of four terpene synthase cDNAs from methyl jasmonate-induced Douglas-fir, Pseudotsuga menziesii". Phytochemistry. 66 (12): 1427–39. doi:10.1016/j.phytochem.2005.04.030. PMID 15921711.

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v t e Carbon–oxygen lyases (EC 4.2) (primarily dehydratases)
4.2.1: Hydro-Lyases	Carbonic anhydrase Fumarase Aconitase Enolase Alpha Enolase 2 Enoyl-CoA hydratase/3-Hydroxyacyl ACP dehydrase Methylglutaconyl-CoA hydratase Tryptophan synthase Cystathionine beta synthase Porphobilinogen synthase 3-Isopropylmalate dehydratase Urocanase Uroporphyrinogen III synthase Nitrile hydratase
4.2.2: Acting on polysaccharides	Hyaluronate lyase Pectin lyase
4.2.3: Acting on phosphates	Threonine synthase
4.2.99: Other	Carboxymethyloxysuccinate lyase Hydroperoxide lyase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)