Most of the natural products isolated at present are heterocyclic compounds, so heterocyclic compounds occupy an important position in the research of organic chemistry. A compound: 542-58-5, is researched, SMILESS is CC(OCCCl)=O, Molecular C4H7ClO2Journal, Article, Research Support, U.S. Gov’t, P.H.S., Journal of Biological Chemistry called Hydrolysis by acetylcholinesterase. Apparent molal volumes and trimethyl and methyl subsites, Author is Hasan, Fariza B.; Cohen, Saul G.; Cohen, Jonathan B., the main research direction is acetylcholinesterase substrate structure activity; hydrophobicity acetylcholinesterase substrate; volume molal acetylcholinesterase substrate.Computed Properties of C4H7ClO2.
A study was made of hydrolysis by acetylcholinesterase (EC 3.1.1.7) and by hydroxide of acetate esters RCH2CH2OCOCH3, where, in the following compounds, R is I, (CH3)3N+; II, (CH3)3; III, (CH3)2NH+; IV, (CH3)2CH; V, CH3NH2+; VI, CH3CH2; VII, NH3+; VIII, CH3; IX, H; X HO; XI, CH3O; XII, Cl; XIII, Br; XIV, CN. Acylation rate constants, k2, are normalized for reactivity in hydrolysis by hydroxide, k(OH). Comparison of Ks within the pairs, III and IV, V and VI, VII and VIII, and probably I and II, and the Ks for X-XIV with V and VII indicates that pos. charge makes little if any contribution to binding. I and II have similar normalized values of k2 and bimol. constants, k2(n)/Ks. IV, VI, and VIII have greater normalized values than the charged analogs III, V, and VII. The effect of pos. charge on kcat and k2 is attributed to the effect on intrinsic reactivity, k(OH). Pos. charge is not specifically activating in acylation and is absent in the very efficient deacylation. The generally accepted anionic site is better considered an uncharged trimethyl site, complementary to substrate (CH3)3X groups. A linear correlation is found between log (k2(n)/Ks) for all 14 compounds and apparent molal volume, V̅0, of the β substituents, R. Enzymic reactivity is determined predominantly by precision of fit of the β substituent in the trimethyl site and the acetyl Me in its Me site, which limits mobility of substrate and desolvates the substrate-enzyme interface.
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