Enolase has a glutamic acid residue in its active site. Describe the experiment that was done that provided evidence for the proposed function of the glutamic acid residue in catalysis by enolase
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Enolase has a glutamic acid residue in its active site. Describe the experiment that was done that provided evidence for the proposed function of the glutamic acid residue in catalysis by enolase.
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- The active site of an enzyme has the following amino acid residues as critical mediators of catalysis: Ser-134, His-347, Tyr-121 and Glu - 406. What are the most likely specific mechanisms of catalysis by these amino acid residues?For a lot of enzymes that work on fatty acids, the rate determining step is the release of the product from the active site. This means that the activation energy for product release is much higher than the free energy of catalysis. What enthalpic or entropic contributions would make the activation energy for product release so high and explain?UDP-glucuronosyltransferase enzymes bind the organic compound UDP-glucuronic acid (UDP-GA) in order to catalyse the transfer of a glucuronic acid group from UDP-GA to a drug molecule, releasing UDP from the active site as a product. UDP is then regenerated by the activity of another enzyme. What terms could be used to describe UDP-GA?
- In what way is the observed mode of action of hexokinase consistent with the induced-fit theory of enzyme action?There is a cysteine protease, which uses a similar chemical mechanism to chymotrypsin except for using cysteine instead of serine during catalysis. Please draw the stepwise chemical mechanism for the cysteine protease.the following is a coenzyme or cofactor involved in enzymatic reaction. identify the biochemical role that S-adenosylmethionine plays within a biochemical tranformation.
- Mevalonate is a component of which biochemical pathway?Trypsin, a peptidase that hydrolyzes polypeptides, functions in the small intestine at an optimum pH of 7.7–8.0. How is the rate of a trypsin-catalyzed reaction affected by each of the following conditions?The formation of a Schiff base in the enzymatically catalyzed decarboxylation of acetoacetate is an example of— electrostatic catalysis. proximity catalysis. covalent catalysis. transition-state catalysis. concerted acid/base catalysis.