inhibition characterized by changes in both Vmax and Km uncompetitive the transition state is formed within this location in an enzyme active site molecules that covalently bind modify active-site...

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Extracted text: inhibition characterized by changes in both Vmax and Km uncompetitive the transition state is formed within this location in an enzyme active site molecules that covalently bind modify active-site residues and are structurally affinity labels similar to substrates used to describe the effects of inhibitors and activators on allosteric enzymes states that enzymes go through conformation changes to catalyze a reaction induced fit between T and R states, the one that is favored by binding enzyme to substrate R state the specific metabolic pathway reaction that ensures product formation Enzyme-substrate enzymes catalyze reactions involving the addition of water hydrolysis the substrate concentration at which V = Vmax/2 Km