Chymotrypsin Mechanism🔥 ll Catalytic triad скачать в хорошем качестве

Chymotrypsin Mechanism🔥 ll Catalytic triad

Chymotrypsin is an enzyme that is used in the small intestine to break down proteins into individual amino acids. Chymotrypsinogen is activated to chymotrypsin in the small intestine by proteolytic cleavage, for instance by trypsin. Chymotrypsin cleaves those peptide bonds in which aromatic amino acids (tyrosine, phenylalanine, and tryptophan) contribute to the carboxyl group. Chymotrypsin uses a better nucleophile in the form of the catalytic triad : Asp 102, His 57, Ser 195 side chains. The transition state is stabilized by the oxyanion hole – Gly 193 and Ser 195 peptide backbone NH groups. The reaction is taken in two easy steps. first step : Acylation Second step : Deacylation & hydolysis The active site of chymotrypsin consists of catalytic triad formed by Aspartate 102 positioned close to histidine 57 and serine 195 if you really want to appreciate my efforts then please like share & subscribe to my channel🙏🙏 #csirnet #chymotrypsin #ankitabiology#neet #csir #lifescience #baayo #education #freeeducation #science #shomusbiology#teachingpathshala