The diagram below shows the substrate binding cleft for a protease, providing the substrate structure, and indicating the residues (using one-letter code) that line the four specificity pockets. F 4 5 2 4 5 2 1 M The protease is known to cleave the amide linkage between W and E residues for substrates containing the WEFD sequence. Of the bonds indicated, which identifies the scissile bond? 3 H₂N 2 3 IN ON F P W
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- a) Based on the mechanism shown in Figure 2A, what type of enzyme is transpeptidase? : Lyase Isomerase Ligase Hydrolase Oxidoreductase Transferase b) Transpeptidases have two substrates. From Figure 2A, what type of mechanism do they most likely adopt in processing the two substrates? sequential or ping-pong c) β-lactams inactivate transpeptidases by forming a covalent bond with the serine residue in the active site. Based on this description and Figure 2B caption, what type of inhibitor are β-lactams? _________________________________________ d) Based on the mechanism for lactamase shown in Figure 3, what type of enzyme is lactamase? Lyase Isomerase Ligase Hydrolase Oxidoreductase Transferase e) Based on your answer in d, what other reactant, in addition to the antibiotic substrate, needs to be in the active site of lactamase for the hydrolysis reaction to proceed? ____________________Discuss that What kind of reaction is catalyzed by each of the followingenzymes?a. citrate decarboxylaseb. oxalate reductasec. serine transaminaseIdentify the type of regulation of enzyme activity seen in the following situations - for example, competitive inhibition, allosterism, phosphorylation, zymogen conversion, association-dissociation, feedback inhibition, etc. a. Trypinsogen, which is not catalytically active, is converted to the active enzyme trypsin by removal of a hexapeptide from the N-terminal end. b. The dimer protein kinases is catalytically inactive. Binding of cAMP causes protein kinase dimer to split into its monomer which are active catalysts.
- 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?The enzyme chymotrypsin, catalyses the hydrolysis of nitrophenyl acetate and pther acyl esters. Name the amino acid residue, the side chain of the residue, and the type of bond/linkage involved in the formation of the acyl-emzyme complex during catalysis.can somone please List the components of the enzyme complex involved in the transition step and Simply describe what does each component does? 1. 2. 3. ect..
- In enzyme catalysed reactions, the energy level of the enzyme/substrate (or ES) complex is higher (or raised) compared to the uncatalyzed reaction. List 4 factors that contribute to this raised energy level and explain how each of these factors contribute to the higher energy level of the ES complexIn the pathway for degradation of BCAAs, which reaction takes place prior to the action of the BCKDC and what is the essential coenzyme for the reaction?Why does it make metabolic sense for UTP to inhibit carbamoyl phosphate synthetase II, whereas ATP activates the enzyme?
- Why is it advantageous for two control mechanisms —allosteric control and covalent modification— to be involved in the metabolism of glycogen?Which of the following regulatory mechanisms will specifically inhibit pyrimidine synthesis (and not also purine synthesis)? (A) allosteric regulation of aspartate transcarbamoylase by CTP(B) allosteric regulation of aspartate transcarbamoylase by ATP(C) synergistic inhibition of PRPP synthetase by AMP/GMP/IMP(D) synergistic inhibition of PRPP amidotransferase by AMP/GMP/IMP (E) feedback inhibition of ribonucleotide reductase by dATPWhat is the evidence that aspartate transcarbamoylase (ATCase) effects catalysis primarily by proximity? In the figure, what is the role of Lys 84' in the active site- interaction that appear to make with the substrate?