1. K m value changes with substrate.The active site of Chymotrysin best accommod
ID: 700622 • Letter: 1
Question
1. Km value changes with substrate.The active site of Chymotrysin best accommodates substrates with a bulky hydrophobic or aromatic residue contributing carbonyl group to peptide bond to be hydrolyzed. Thus, Km varies with the bulkiness of the substrate molecule that is encounters.
2. Km and Vmax are inter-related to enzyme kinetics. Km is that substrate concentration which is required for the reaction to occur at 1/2 the value of Vmax. In other words, it is how much substrate is needed for the reaction to occur at 1/2 its max possible rate. Obviously Vmax is the maximum rate that the reaction can proceed at. Thus, Vmax also changes with substrate.
3. The value of Km doesn't change much concentration or pH.
Explanation / Answer
Chymotrypsin serves as a catalyst in the "Hydrolysis" of pepdite bonds - found in carboxylic groups of amino acids, which consist of aromatic pedand groups and large hydrophobic groups. Chymotrypsin is also known to serve as a catalyst in the Hydrolysis of "ester - and amide bonds" , found in hydrophobic groups. 1. Would you expect the KM of the reactions of Chymotrypsin with the different substrates to have the same value ? explain your reasoning. 2. Would you expect the Vmax of the reactions of Chymotrypsin with the different substrates to have the same value ? explain your reasoning. 3. Would you expect the " pH-dependence " of the "hydrolysis - reactions" of the different substrates to be the same for all substrates ? explain your reasoning.
Related Questions
Navigate
Integrity-first tutoring: explanations and feedback only — we do not complete graded work. Learn more.