BCH 4054 Lecture Notes - Lecture 23: Serine Protease, Catalytic Triad, Covalent Bond
Document Summary
Serine protease- involved in digesion, blood cloing and inlammaion. Elastase- cleaves ater ala, gly, ser and val. These are the smaller, neutral residues of the amino acids. Dipf reacts with the acive site of serine protease to inacive the enzyme. Catalyic triad- can determine which amino acids are important. S analog will bind to the acive site to form a covalent bond. Reacion kineics- basically studying the reacion rate. This is the conversion of the substrate to product in a certain period of ime (molar per second or millimolar per second) Michealis-menten kineics- determines the reacion velocity under the assumpion that the enzyme isn"t inhibited by the amount of product and the enzyme is not going to deacivate during the reacion. T is the ime for half the reactant to decompose. Michaelis-menten kineic equaion is for single substrate reacions. The equaion can tell you the eiciency of the enzymes for catalyze get the reacion.
