Sandbox Reserved 987: Difference between revisions

Cocaine Esterase is a globular protein that is expressed in the cytosol of ''Rhodococcus'' strain of bacteria, containing 574 residues divided into three domains. Domain I is a α/β hydrolase fold-containing domain consisting of residues 1-144 and residues 241-354 with the active site His-287. Domain II is a α-helical consisting of residues 145-240, making up seven helices inserted between β6 and β7 of Domain I. Helices two through six together form a five helix core with helices two and three combine to make a lid-like structure over the active site, His-287. Domain III is made up of residues 355-574 with mostly β-structure and a β-barrel-like core connected by 6 cross over loops, forming a jelly roll-like topology.^{<ref>Narasimhan, D.; Woods, J.H.; Sunahara, R.K. “Bacterial cocaine esterase: a protein-based therapy for cocaine overdose and addiction.” ''Future Med Chem.'' 2012, 4, 2: 137-150.</ref>}

Cocaine esterase is used to catalyze the following reaction:

cocaine + H₂O ←→ ecgonine methyl ester + benzoate <sup><ref>Cocaine esterase

From Wikipedia, the free encyclopedia</ref></sup>

Cocaine esterase works in a three step mechanism shown below:^{<ref>Liu J., Zhao X., Yang W., Zhan G. C. (2011) Reaction mechanism for cocaine esterase-catalyzed hydrolysis of (+)- and (-)-cocaine: unexpected common rate-determining step. J. Phys. Chem. B. 115(17), 5017-5025.</ref>}