Substrate-Selective Inhibition and Peripheral Site Labeling of Acetylcholinesterase by Platinum(Terpyridine)Chloride

Autor:	Terrone L. Rosenberry, Robert Haas, Mark A. Rosenberry, Elizabeth W. Adams
Rok vydání:	1992
Předmět:	biology Affinity label Inorganic chemistry Substrate (chemistry) Medicinal chemistry Acetylcholinesterase Catalysis Hydrolysis chemistry.chemical_compound Reaction rate constant chemistry medicine biology.protein Enzyme kinetics Acetylcholine medicine.drug
Zdroj:	Multidisciplinary Approaches to Cholinesterase Functions ISBN: 9781461363286
DOI:	10.1007/978-1-4615-3046-6_18
Popis:	Acetylcholinesterase (AChE) catalyzes the hydrolysis of its physiological substrate acetylcholine as well as of a number of other acetic acid esters. A key feature of AChE is its speed in cleaving substrates (Rosenberry, 1975a). The second order rate constant for acetylcholine hydrolysis (kcat/Kapp = 2 × 108 M-1s-1) approaches the value expected for a diffusion-controlled reaction. The turnover rate for acetylcholine (kcat = 2 x 104 s-1) is at the upper limit of reactions catalyzed by general acid-base catalysis. Quinn (1987) has noted that an enzyme with such a high catalytic efficiency is likely to have evolved to a point where the free energies of successive transition states are nearly matched and comparable to the diffusional barrier for substrate binding.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::7eecb77a44b8294a28dfb250cb8d6434 https://doi.org/10.1007/978-1-4615-3046-6_18 Zobrazit plný text záznamu