Question

PIS) I Many protease enzymes have Cys-His-Asp catalytic triad. Draw the resting state of the active site of an enzyme with this kind of catalytic triad. Draw plausible tetrahedral intermediates (two structures needed) for hydrolysis of the peptide bond shown below. Ro-N^ RN

Answer 1

structure with triad catalys Ans. Proteases. catalytic tocad Nucleoplulia Cserine Nu AN AN 3ase en Histidine Aciden- ASP Semilys symmary enzyme - These the stact and active site of the proteases anzymes. gelen past that indicate in the structure is the active part of protease Histidine is abase Aspartate is the acid and the nucleephilic is the berine Catalytic triad mostly found in Proteases & Carides, esferase acglase, lipase & ß-lactamase These triad Asp-has-cys are Covalently attached.. . .

tetrahedral intermediate for peptide bond hydrolysis Ram Covalentalyst Sess The protease) Acid -base Catalyans CASP? NOC NH Base C - NH Acid loh Асс Tetrahedral intermediates Acid Base synmary Formed during peptide cleanege & Protease enzyme. . It accelerate the transition fate of peptide bond hydrolysis In the process of cys, ser, protease, covalent bond are stase with enzyme catalytic jyeu llophilic» Is Asp case, the non covalent bond, Aeid- base mechanism where done. in tetrahedral bond, it is difficult to invent the chemical structure so that chemist on Protein enggineer difficult to eat efficiently catalyst the peptide bond cleanase