Patchoulol synthase

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Patchoulol synthase
Patchoulol synthase
Identifiers
EC no.	4.2.3.70
Databases
BRENDA	enzyme data
ExPASy	NiceZyme view
KEGG	enzyme entry
MetaCyc	metabolic pathway
Rhea	reactions
PDB structures	RCSB PDB PDBe PDBsum
PMC
Search
PMC	articles
PubMed	articles
NCBI	proteins

Patchoulol synthase (EC 4.2.3.70) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase (patchoulol-forming). This enzyme catalyses the following chemical reaction

(2E,6E)-farnesyl diphosphate + H₂O

\rightleftharpoons

patchoulol + diphosphate

References

↑ Croteau R, Munck SL, Akoh CC, Fisk HJ, Satterwhite DM (July 1987). "Biosynthesis of the sesquiterpene patchoulol from farnesyl pyrophosphate in leaf extracts of Pogostemon cablin (patchouli): mechanistic considerations". Archives of Biochemistry and Biophysics. 256 (1): 56–68. doi:10.1016/0003-9861(87)90425-5. PMID 3038029.
↑ Munck SL, Croteau R (October 1990). "Purification and characterization of the sesquiterpene cyclase patchoulol synthase from Pogostemon cablin". Archives of Biochemistry and Biophysics. 282 (1): 58–64. doi:10.1016/0003-9861(90)90086-e. PMID 2171435.
↑ Faraldos JA, Wu S, Chappell J, Coates RM (March 2010). "Doubly deuterium-labeled patchouli alcohol from cyclization of singly labeled [2-²H₁]farnesyl diphosphate catalyzed by recombinant patchoulol synthase". Journal of the American Chemical Society. 132 (9): 2998–3008. Bibcode:2010JAChS.132.2998F. doi:10.1021/ja909251r. PMID 20148554.

External links

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

[1] Croteau R, Munck SL, Akoh CC, Fisk HJ, Satterwhite DM (July 1987). "Biosynthesis of the sesquiterpene patchoulol from farnesyl pyrophosphate in leaf extracts of Pogostemon cablin (patchouli): mechanistic considerations". Archives of Biochemistry and Biophysics. 256 (1): 56–68. doi:10.1016/0003-9861(87)90425-5. PMID 3038029.

[2] Munck SL, Croteau R (October 1990). "Purification and characterization of the sesquiterpene cyclase patchoulol synthase from Pogostemon cablin". Archives of Biochemistry and Biophysics. 282 (1): 58–64. doi:10.1016/0003-9861(90)90086-e. PMID 2171435.

[3] Faraldos JA, Wu S, Chappell J, Coates RM (March 2010). "Doubly deuterium-labeled patchouli alcohol from cyclization of singly labeled [2-²H₁]farnesyl diphosphate catalyzed by recombinant patchoulol synthase". Journal of the American Chemical Society. 132 (9): 2998–3008. Bibcode:2010JAChS.132.2998F. doi:10.1021/ja909251r. PMID 20148554.

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 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 Thebaine synthase

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)