2578-84-9Relevant articles and documents
Catalysis in peptide synthesis with active esters. I. Bifunctional catalysis in the aminolysis of benzyloxycarbonyl-L-phenylalanine p-nitrophenyl ester in dioxane.
Nakamizo
, p. 1071 - 1077 (1969)
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Synthesis and evaluation of peptidic irreversible inhibitors of tissue transglutaminase
Pardin, Christophe,Gillet, Steve M.F.G.,Keillor, Jeffrey W.
, p. 8379 - 8385 (2008/02/05)
Herein we report the synthesis and the evaluation of eight novel compounds as irreversible inhibitors of transglutaminase (TGase). These compounds are based on a minimal peptidic scaffold shown previously [Chem. Biol. 2005, 12, 469-475] to confer affinity for the TGase active site and bear electrophilic groups such as α,β-unsaturated amide, chloroacetamide or maleimide; their general structure being Cbz-Phe-spacer-electrophile. The affinity conferred by the Cbz-Phe scaffold was determined by comparison to N-propylacrylamide and the length of the spacer was also varied to evaluate its importance. The inhibitory efficiencies (kinact/KI) of these compounds vary up to 105 M-1 min-1, among the highest reported for derivatives based on this simple Cbz-Phe peptidic scaffold.
Fairly marked enantioselectivity for the hydrolysis of amino acid esters by chemically modified enzymes
Yano, Yoshihiro,Shimada, Kenji,Okai, Jiro,Goto, Koichi,Matsumoto, Yoko,Ueoka, Ryuichi
, p. 1314 - 1318 (2007/10/03)
The hydrolysis (deacylation) of enantiomeric substrates by the chemically modified enzymes decanoyl-α-chymotrypsin and decanoyl-trypsin was studied. Reaction activity for decanoyl-α-chymotrypsin was lower than that for the native enzyme, although intriguingly the enantioselectivity was markedly enhanced as compared with the native enzyme. In particular, the apparently complete enantioselective catalysis was attained for the hydrolytic cleavage of p-nitrophenyl N-dodecanoyl- D(L)-phenylalaninates. The enhancement of enantioselectivity, however, was not observed for decanoyl-trypsin. These results suggest that the chemically modified α-chymotrypsin by addition of hydrophobic groups has promoted enantioselectivity for the hydrolysis of hydrophobic esters.