Detail of "18439-24-2"

Reference

A new method of specific acylation of thiols

A new method of specific acylation of thiols. Application to coenzyme A. Le Goffic, F.; Sicsic, S.; Vincent, Ch. (Cent. 18439-24-2 and 85-61-0 are cas registry numbers. These chemicals are also mentioned in this article. Etud. Rech. Chim. Org. Appl., CNRS, Thiais, Fr.). Tetrahedron Lett., (33), 2845-7 (French) 1976. CODEN: TELEAY. DOCUMENT TYPE: Journal CA Section: 33 (Carbohydrates) Section cross-reference(s): 34 CoA and its trilithium salt with Ac2O and membrane-insolubilized pyridine gave, after lyophilization, 95% S-acetylcoenzyme A. S-succinoylcoenzyme A, S-acetylglutathione, and N,S-diacetylcysteine were prepd. similarly in 88-95% yield. .

Substrate Binding and Catalytic Mechanism of Human Choline Acetyltransferase

All Rights Reserved. Substrate Binding and Catalytic Mechanism of Human Choline Acetyltransferase. Kim, Ae-Ri; Rylett, R. Jane; Shilton, Brian H. (Department of Biochemistry and Physiology and Pharmacology, Schulich School of Medicine and Dentistry, University of Western Ontario, London, ON, Can.). Biochemistry, 45(49), 14621-14631 (English) 2006 American Chemical Society. CODEN: BICHAW. ISSN: 0006-2960. DOCUMENT TYPE: Journal CA Section: 7 (Enzymes) Section cross-reference(s): 75 Choline acetyltransferase (ChAT) catalyzes the synthesis of the neurotransmitter acetylcholine from choline and acetyl-CoA, and its presence is a defining feature of cholinergic neurons. We report the structure of human ChAT to a resoln. of 2.2 ? along with structures for binary complexes of ChAT with choline, CoA, and a nonhydrolyzable acetyl-CoA analog, S-(2-oxopropyl)-CoA. The ChAT-choline complex shows which features of choline are important for binding and explains how modifications of the choline trimethylammonium group can be tolerated by the enzyme. A detailed model of the ternary Michaelis complex fully supports the direct transfer of the acetyl group from acetyl-CoA to choline through a mechanism similar to that seen in the serine hydrolases for the formation of an acyl-enzyme intermediate. Domain movements accompany CoA binding, and a surface loop, which is disordered in the unliganded enzyme, becomes localized and binds directly to the phosphates of CoA, stabilizing the complex. 78-95-5 and 18439-24-2 are just another two chemicals used in this study. Interactions between this surface loop and CoA may function to lower the KM for CoA and could be important for phosphorylation-dependent regulation of ChAT activity. .