α-muurolene synthase | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
EC no. | 4.2.3.125 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
|
α-Muurolene synthase (EC 4.2.3.125, Cop3) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase (cyclizing, α-muurolene-forming). This enzyme catalyses the following chemical reaction
- (2E,6E)-farnesyl diphosphate α-muurolene + diphosphate
The enzyme has been characterized from the fungus Coprinus cinereus.
References
- 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.
- 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
- Alpha-muurolene+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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 | |
---|---|
Activity | |
Regulation | |
Classification | |
Kinetics | |
Types |
|