Beginning with the 1st tetrahedral intermediate, show the complete steps in chymotrypsin mechanism that occurs to form the 2nd chymotrypsin intermediate in the chymotrypsin active site. The substrate for chymotrypsin to be used is Ala-Tyr-Gly. Further, name the amino acid(s) that would be released as a result of the reactions you'd illustrated above.
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Beginning with the 1st tetrahedral intermediate, show the complete steps in chymotrypsin mechanism that occurs to form the 2nd chymotrypsin intermediate in the chymotrypsin active site. The substrate for chymotrypsin to be used is Ala-Tyr-Gly.
Further, name the amino acid(s) that would be released as a result of the reactions you'd illustrated above.
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- Using the ActiveModel for aldose reductase, describe the structure of the TIM barrel motif and the structure and location of the active site.The hydrolysis of a phenylalanine-containing peptide is catalyzed by a-chymotrypsin with the following results. Calculate KM and Vmax for the reaction. What is the equation of the line?Why might the compound shown below act as a transition state analog of phosphoglucose isomerase? A drawing of the normal transition state for this enzyme is needed.
- In many biochemical reactions which involves the formation of an enolate intermediate, the carbonyl oxygen of the substrate is coordinated to a divalent metal ion (usually zinc or magnesium) in the active site. Explain with structural drawings, how this ion-dipole interactions affect the acidity of the a-protons?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?Given each set of information which may include common name(s) and the reaction catalyzed, you are required to identify the main class of the specific enzyme described. _____________________1. Name: alkaline phosphataseReaction: a phosphate monoester + H2O = an alcohol + phosphate_____________________2. Reaction: L-threonine = D-threonine.Other information: Inverts both chiral centers, a racemase. _____________________3. Name: glycine-N-acylaseReaction: acyl-COA + glycine = CoA + N-acylglycine_____________________ 4. Name: lysine decarboxylaseReaction: L-lysine = cadaverine + CO2 _____________________5. Name: methanol dehydrogenaseReaction: methanol + NAD+ = formaldehyde + NADH + H+ _____________________6. Name: citryl-CoA synthetaseReaction: ATP + citrate + CoA = ADP + phosphate + (3S)-citryl-CoA_____________________7. Name: D-xylulose reductaseReaction: xylitol + NAD+ = D-xylulose + NADH + H+ _____________________8. Name: cellobiose phosphorylaseReaction: cellobiose phosphate =…
- The glycine cleavage system is a group of four enzymes that together catalyze the following reaction: Use the following information to determine the sequence of reactions carried out by the glycine cleavage system:a. The first enzyme is a PLP-requiring decarboxylase.b. The second enzyme is aminomethyltransferase. This enzyme has a lipoate coenzyme.c. The third enzyme synthesizes N5,N10-methylene-THF and also forms +NH4.d. The fourth enzyme is an FAD-requiring enzyme.e. The cleavage system also requires NAD+ .What kind of inhibitor is threo-sphingosine? Explain this type of inhibition.Which of the following statements is not true about the catalytic triad in chymotrypsin? Group of answer choices the side chain of the serine 195 is hydrogen bonded to the imidazole ring of histidine the -NH group of the imidazole ring of histidine is hydrogen bonded to the carboxylate group of aspartate 102 the histidine residue serves to position the aspartate 102 side chain and to polarize its carboxylate group so that it is poised for deprotonation histidine acts as a general base catalyst none of these
- 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?What are the possivble oxidation product of catalase using H2O2 as the substrate? Explain in 1-3 sentencesThe KM for the reaction of chymotrypsin with N-acetylvaline ethyl ester is 8.8 × 10−2 M, and the KM for the reaction of chymotrypsin with N-acetyltyrosine ethyl ester is 6.6 × 10−4 M. (a) Which substrate has the higher apparent affi nity for the enzyme? (b) Which substrate is likely to give a higher value for Vmax?