Final answer:
O-octanoyl groups from proteins are removed by an esterase, which hydrolyzes ester linkages involving a carboxyl group and a hydroxyl group from a serine residue. Pancreatic lipase is not effective for this removal as its primary role pertains to lipid breakdown, and the specific class of enzymes for hydrolysis of such esters in proteins are hydrolases, specifically esterases.
Step-by-step explanation:
The enzyme commonly associated with the removal of O-octanoyl groups from proteins is an esterase. The linkage typically present between the serine residue and the O-octanoyl group is an ester linkage. Pancreatic lipases are not effective in removing O-octanoyl groups from proteins as they mainly break down dietary fats. The enzyme class specifically designed for the hydrolysis of ester linkages in proteins is the hydrolase class, particularly esterases. In the context of protein modification, the primary role of lipases is breaking down lipids, rather than modifying protein groups.The O-octanoyl modification, being an ester linkage, involves a carboxyl group from the O-octanoyl moiety and a hydroxyl group of a serine residue in the protein. The specific term for enzymes that catalyze the hydrolysis of ester linkages in proteins is esterase.
The enzyme commonly associated with the removal of O-octanoyl groups from proteins is lipase.The type of linkage typically present between the serine residue and the O-octanoyl group is an ester linkage.Pancreatic lipase cannot effectively remove O-octanoyl groups from proteins as its main function is to break down lipids.The enzyme class specifically designed for the hydrolysis of ester linkages in proteins is esterase.In the context of protein modification, the primary role of lipases is to break down lipids.The O-octanoyl modification involves an ester linkage, which means the carboxyl group is involved in this linkage.The specific term for enzymes that catalyze the hydrolysis of ester linkages in proteins is esterase.