943531-07-5

Upstream product

• 943531-12-2 N-benzyloxycarbonyl-S-(p-nitrophenyloxycarbonyl)-L-cysteinylglycine tert-butyl ester 
• 191151-92-5 {(R)-2-Benzyloxycarbonylamino-3-[(R)-2-benzyloxycarbonylamino-2-(tert-butoxycarbonylmethyl-carbamoyl)-ethyldisulfanyl]-propionylamino}-acetic acid tert-butyl ester 
• 501-53-1 benzyl chloroformate 
• 6968-11-2 N,N'-bis(benzyloxycarbonyl)-L-cystine 
• 1013328-76-1 N-benzyloxycarbonyl-L-cysteinylglycine tert-butyl ester 

Relevant academic research and scientific papers

Acyl transfer from carboxylate, carbonate, and thiocarbonate esters to enzymatic and nonenzymatic thiolates

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.