A medicinal chemist is trying to determine the mechanism of action of inhibitors she has synthesized. The relative change in KM and Vmax upon incubation of the targeted enzyme with each inhibitor is shown in the table below.

Examine this depiction of the initial steps of catalysis for a proteolytic enzyme. Oxyanion hole 93 with In 1-2 sentences, describe the role being played by the amino acid hydroxyl side chain in the step labeled 2. In 1-2 sentences, describe the role of the oxyanion hole. In 1-2 sentences, describe the role of the His is the step labeled 3.

29. In chymotrypsin both histidine and serine are important amino acids in the catalytic reaction. Below is an image showing one step of the reaction. Describe what is happening and the roles histidine and serine are playing. In your answer be sure to use correct terms in describing the type of enzyme mechanism being done each amino acid. His Asp 102 H₂C CH₂ Ser (195) CH₂ 4 Asp 102 H₂C CH₂ His 57 New N-terminus of cleaved polypeptide R chain Ser 195 CH₂

help please answer in text form with proper workings and explanation for each and every part and steps with concept and introduction no AI no copy paste remember answer must be in proper format with all working

An enzyme catalyzes the reaction M ⇌ N. The enzyme is present at a concentration of 1 nM, and the Vmax is 2 μM s−1. The Km for substrate M is 4 μM. (a) Calculate kcat. (b) What values of Vmax and Km would be observedin the presence of sufficient amounts of an uncompetitive inhibitor to generate an α′ of 2.0?

Trypsin is a serine protease that has a KM of 15 mM. At an initial substrate concentration of 250 µM insulin, trypsin is found to degrade insulin at a rate of 0.6 µM/min. If the concentration of trypsin in solution was 4.326 µM, what is the kcat of trypsin in s-1?

Question #44