Tropinesterase
| tropinesterase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.1.1.10 | ||||||||
| CAS no. | 59536-71-9 | ||||||||
| 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 / QuickGO | ||||||||
| |||||||||
In enzymology, a tropinesterase (EC 3.1.1.10) is an enzyme that catalyzes the chemical reaction
- atropine + H2O tropine + tropate
Thus, the two substrates of this enzyme are atropine and H2O, whereas its two products are tropine and tropate.
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is atropine acylhydrolase. Other names in common use include tropine esterase, atropinase, and atropine esterase.
References
- Glick D, Glaubach S, Moore DH (1942). "Azolesterase activities of electrophoretically separated proteins of serum". J. Biol. Chem. 144: 525–528.
- Moog P, Krisch K (1974). "[The purification and characterization of atropine esterase from rabbit liver microsomes (author's transl)]". Hoppe-Seyler's Z. Physiol. Chem. 355 (5): 529–42. PMID 4435736.
