191151-92-5Relevant academic research and scientific papers
Acyl transfer from carboxylate, carbonate, and thiocarbonate esters to enzymatic and nonenzymatic thiolates
Gravel, Christian,Lapierre, Danielle,Labelle, Judith,Keillor, Jeffrey W.
, p. 164 - 174 (2008/02/13)
Transglutaminases (EC 2.3.2.13) (TGases) catalyze calcium-dependent acyl transfer reactions between peptide-bound glutamine residues as acyl donors and peptide-bound lysine residues as acyl acceptors, resulting in the formation of intermolecular ε-(γ-glutamyl)lysine crosslinks. The mechanistic details of its "ping-pong" transamidation reaction remain unknown. In particular, few studies have been published probing the nucleophilicity of TGase using acyl-donor substrates of varied electrophilicity. Herein we report the synthesis of activated esters of carbonates, carbamates, and thiocarbonates and their reactions with simple thiols, as a nonenzymatic point of reference, and with the catalytic cysteine residue of guinea pig liver TGase. Our kinetic results show that the simple substitution of a side chain methylene unit by oxygen or sulphur had a surprising effect on both substrate affinity and acylation reactivity. Furthermore, they provide unexpected insight into the importance of a side chain heteroatom for conferring affinity for tissue TGase as well as revealing an interesting class of irreversible inhibitors.
Peptide Synthesis at High Pressure: Activation Volume of a Peptide Coupling, Synthesis of a Glutathione Derivative
Klaerner, Frank-Gerrit,Kalthof, Ulrike,Gante, Joachim
, p. 359 - 364 (2007/10/03)
From the pressure-induced rate enhancement the activation volume of the peptide coupling 1 with the sodium salt of glycine 2 leading to the corresponding dipeptide derivative 3 was determined to be strongly negative (ΔV≠ = -(19.3 ± 0.5) cm
