17663-35-3Relevant articles and documents
High Stereoselectivity in the Deacylation of p-Nitrophenyl N-Acylphenylalanates by Bilayer Vesicular Systems which include Dipeptide-type Nucleophiles
Ohkubo, Katsutoshi,Matsumoto, Noriko,Ohta, Hidefumi
, p. 738 - 740 (1982)
The deacylation of p-nitrophenyl N-acylphenylalanates with bilayer vesicular systems comprising dipeptide-type nucleophiles and a cationic double chain surfactant resulted in high stereoselectivity (kLcat/kDcat = 29.6 at 25 deg C and 83.6 at 10 deg C) for the deacylation of p-nitrophenyl N-dodecanoylphenylalanate by the catalytic system of N-(N-benzyloxycarbonyl-L-leucyl)-L-histidine and N,N-didodecyl-N,N-dimethylammonium bromide.
Designed Negative Feedback from Transiently Formed Catalytic Nanostructures
Afrose, Syed Pavel,Bal, Subhajit,Chatterjee, Ayan,Das, Krishnendu,Das, Dibyendu
, p. 15783 - 15787 (2019)
Highly dynamic and complex systems of microtubules undergo a substrate-induced change of conformation that leads to polymerization. Owing to the augmented catalytic potential at the polymerized state, rapid hydrolysis of the substrate is observed, leading to catastrophe, thus realizing the out-of-equilibrium state. A simple synthetic mimic of these dynamic natural systems is presented, where similar substrate induced conformational change is observed and a transient helical morphology is accessed. Further, augmented catalytic potential of these helical nanostructures leads to rapid hydrolysis of the substrate providing negative feedback on the stability of the nanostructures and realization of an out-of-equilibrium state. This simple system, made from amino acid functionalized lipids, demonstrates a substrate-induced self-assembled state, where the fuel-to-waste conversion leads to the temporal presence of helical nanostructures.
Kinetic study on conformational effect in hydrolysis of p-nitroanilides catalyzed by α-chymotrypsin
Kawai, Yasushi,Matsuo, Takashi,Ohno, Atsuyoshi
, p. 887 - 891 (2007/10/03)
Effects of medium viscosity on kinetics for the hydrolysis of p-nitroanilides of certain amino acid derivatives catalyzed by α-chymotrypsin have been investigated. Observed data indicate that the overall rate constant, kcat, is hardly affected by the medium viscosity in all the substrates employed and equals the rate constant at the acylation step, k2, in the measured range of viscosity. By comparison with the data on p-nitrophenyl ester substrates reported previously, it is concluded that the formation of the tetrahedral intermediate in the course of the acylation of the enzyme is influenced by conformational change of the enzyme, whereas the breakdown of the intermediate is almost free from conformational effects.
Synthesis of glutamate receptor antagonist philanthotoxin-433 (PhTX-433) and its analogs
Goodnow Jr.,Konno,Niwa,Kallimopoulos,Bukownik,Lenares,Nakanishi
, p. 3267 - 3286 (2007/10/02)
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