Pazy, Yael; Raboy, Bilha; Matto, Meirav; Bayer, Edward A.; Wilchek, Meir; Livnah, Oded published the artcile< Structure-based rational design of streptavidin mutants with pseudo-catalytic activity>, Application of C19H34O2, the main research area is design streptavidin hydrolysis catalyst.
Introduction of enzymic activity into proteins or other types of polymers by rational design is a major objective in the life sciences. To date, relatively low levels of enzymic activity could be introduced into antibodies by using transition-state analogs of haptens. In the present study, the authors identify the structural elements that contribute to the observed hydrolytic activity in egg white avidin, which promote the cleavage of active biotin esters (notably biotinyl p-nitrophenyl ester). The latter elements were then incorporated into bacterial streptavidin via genetic engineering. The streptavidin mol. was thus converted from a protector to an enhancer of hydrolysis of biotin esters. The conversion was accomplished by the combined replacement of a “”lid-like loop”” (L3,4) and a leucine-to-arginine point mutation in streptavidin. Interestingly, neither of these elements play a direct role in the hydrolytic reaction. The latter features were thus shown to be responsible for enhanced substrate hydrolysis. This work indicates that structural and noncatalytic elements of a protein can be modified to promote the induced fit of a substrate for subsequent interaction with either a catalytic residue or water mols. This approach complements the conventional design of active sites that involves direct modifications of catalytic residues.
Journal of Biological Chemistry published new progress about Avidins Role: BSU (Biological Study, Unclassified), PRP (Properties), BIOL (Biological Study). 112-63-0 belongs to class esters-buliding-blocks, and the molecular formula is C19H34O2, Application of C19H34O2.
Referemce:
Ester – Wikipedia,
Ester – an overview | ScienceDirect Topics