{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,19]],"date-time":"2026-06-19T02:11:37Z","timestamp":1781835097339,"version":"3.54.5"},"reference-count":58,"publisher":"MDPI AG","issue":"9","license":[{"start":{"date-parts":[[2024,5,4]],"date-time":"2024-05-04T00:00:00Z","timestamp":1714780800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100012528","name":"Kazan Federal University","doi-asserted-by":"publisher","award":["Priority 2030"],"award-info":[{"award-number":["Priority 2030"]}],"id":[{"id":"10.13039\/501100012528","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100012528","name":"Kazan Federal University","doi-asserted-by":"publisher","award":["BT\/INF\/22\/SP45375\/2022"],"award-info":[{"award-number":["BT\/INF\/22\/SP45375\/2022"]}],"id":[{"id":"10.13039\/501100012528","id-type":"DOI","asserted-by":"publisher"}]},{"name":"DBT Builder Interdisciplinary Project, Govt. of India","award":["Priority 2030"],"award-info":[{"award-number":["Priority 2030"]}]},{"name":"DBT Builder Interdisciplinary Project, Govt. of India","award":["BT\/INF\/22\/SP45375\/2022"],"award-info":[{"award-number":["BT\/INF\/22\/SP45375\/2022"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecules"],"abstract":"<jats:p>The participation of butyrylcholinesterase (BChE) in the degradation of atropine has been recurrently addressed for more than 70 years. However, no conclusive answer has been provided for the human enzyme so far. In the present work, a steady-state kinetic analysis performed by spectrophotometry showed that highly purified human plasma BChE tetramer slowly hydrolyzes atropine at pH 7.0 and 25 \u00b0C. The affinity of atropine for the enzyme is weak, and the observed kinetic rates versus the atropine concentration was of the first order: the maximum atropine concentration in essays was much less than Km. Thus, the bimolecular rate constant was found to be kcat\/Km = 7.7 \u00d7 104 M\u22121 min\u22121. Rough estimates of catalytic parameters provided slow kcat &lt; 40 min\u22121 and high Km = 0.3\u20133.3 mM. Then, using a specific organophosphoryl agent, echothiophate, the time-dependent irreversible inhibition profiles of BChE for hydrolysis of atropine and the standard substrate butyrylthiocholine (BTC) were investigated. This established that both substrates are hydrolyzed at the same site, i.e., S198, as for all substrates of this enzyme. Lastly, molecular docking provided evidence that both atropine isomers bind to the active center of BChE. However, free energy perturbations yielded by the Bennett Acceptance Ratio method suggest that the L-atropine isomer is the most reactive enantiomer. In conclusion, the results provided evidence that plasma BChE slowly hydrolyzes atropine but should have no significant role in its metabolism under current conditions of medical use and even under administration of the highest possible doses of this antimuscarinic drug.<\/jats:p>","DOI":"10.3390\/molecules29092140","type":"journal-article","created":{"date-parts":[[2024,5,6]],"date-time":"2024-05-06T13:27:00Z","timestamp":1715002020000},"page":"2140","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":6,"title":["Human Plasma Butyrylcholinesterase Hydrolyzes Atropine: Kinetic and Molecular Modeling Studies"],"prefix":"10.3390","volume":"29","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-5806-6104","authenticated-orcid":false,"given":"Aliya","family":"Mukhametgalieva","sequence":"first","affiliation":[{"name":"Laboratory of Biochemical Neuropharmacology, Kazan Federal University, Kremlevskaya Str. 18, 420008 Kazan, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3668-2184","authenticated-orcid":false,"given":"Showkat Ahmad","family":"Mir","sequence":"additional","affiliation":[{"name":"School of Life Sciences, Sambalpur University, Jyotivihar, Burla 768019, India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0008-5713-4137","authenticated-orcid":false,"given":"Zukhra","family":"Shaihutdinova","sequence":"additional","affiliation":[{"name":"Laboratory of Biochemical Neuropharmacology, Kazan Federal University, Kremlevskaya Str. 18, 420008 Kazan, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7837-3662","authenticated-orcid":false,"given":"Patrick","family":"Masson","sequence":"additional","affiliation":[{"name":"Laboratory of Biochemical Neuropharmacology, Kazan Federal University, Kremlevskaya Str. 18, 420008 Kazan, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2024,5,4]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"Shim, K.H., Kang, M.J., Sharma, N., and An, S.S.A. 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