Aristolochene synthase
| aristolochene synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 4.2.3.9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / EGO | ||||||||
|
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In enzymology, an aristolochene synthase (EC 4.2.3.9) is an enzyme that catalyzes the chemical reaction
aristolochene + diphosphateHence, this enzyme has one substrate, 2-trans,6-trans-farnesyl diphosphate, and two products, aristolochene and diphosphate.
This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on phosphates. The systematic name of this enzyme class is 2-trans,6-trans-farnesyl-diphosphate diphosphate-lyase (cyclizing, aristolochene-forming). Other names in common use include sesquiterpene cyclase, trans,trans-farnesyl diphosphate aristolochene-lyase, trans,trans-farnesyl-diphosphate diphosphate-lyase (cyclizing,, and aristolochene-forming). This enzyme participates in terpenoid biosynthesis.
This protein may use the morpheein model of allosteric regulation.[1]
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2E4O and 2OA6. They are both notable for the very high helix content of the structure.
References
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