The enzyme tropinesterase (EC 3.1.1.10) catalyzes the reaction
| 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 | ||||||||
| |||||||||
- atropine + H2O tropine + tropate
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is atropine acylhydrolase. Other names in common use include tropine esterase, atropinase, and atropine esterase.
In animal
editReferences
edit- ↑ Harrison, Patrick K.; Tattersall, John E. H.; Gosden, Ed. "The presence of atropinesterase activity in animal plasma". Naunyn-Schmiedeberg's Archives of Pharmacology. 373 (3): 230–236. doi:10.1007/s00210-006-0054-5. ISSN 0028-1298. PMID 16736160.
- Glick D, Glaubach S, Moore DH (1942). "Azolesterase activities of electrophoretically separated proteins of serum". J. Biol. Chem. 144 (2): 525–528. doi:10.1016/S0021-9258(18)72538-6.
- 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.
 | This EC 3.1 enzyme-related article is a stub. You can help Wikipedia by adding missing information. |