A protein degrading enzyme found in the liver of cows protea

A protein degrading enzyme found in the liver of cows (protease Moo1) is activated (functional) by covalently attaching a phosphate group to a tyrosine (a neutral charged amino acid) in the middle of the enzyme. In pigs, the corresponding liver enzyme (protease Oink1) has an aspartic acid (strongly negatively charged amino acid) instead of the tyrosine found in the middle of the cow enzyme. The pig enzyme is active all of the time. Why? What is happening to the protein structure in the cow enzyme when the phosphate group is added?

Solution

The significant serine proteases geometry with tyrosine is enable them to recognize the substrate cleavage sites and they characteristically bind at the transition state, finally declines the overall activation energy of the reaction, and thereby enables the significant catalytic ability of the enzyme.

Phosphate addition is going to trigger \"phosphorylation of active siute in the protein structure in the cow enzyme\" when the phosphate group is added finally causes \"conformation change of active site. This going to takes place by covalently attaching a phosphate group to a tyrosine (a neutral charged amino acid) in the middle of the enzyme so that it going to rapidly bound to the \"protein substrates\" finally reduces activation energy of substrate to convert into products. The activity is only pertaining to tyrosine is mainly induce a catalytic triad formation at certain pH along with serine proteases Moo1 and active at certain physiological pH. The corresponding liver enzyme (protease Oink1) in pigs has an aspartic acid (strongly negatively charged amino acid) i.e. \"aspartyl proteases\" active at all times because it can induce cow enzyme. The pig enzyme is active all of the time because they have two \"meticulously conserved aspartates\" in their active site so that it can be active at acidic pH finally generate oxyanion hole & to cause a nucleophilic attack on the proteins