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- Protease enzymes cleave proteins by hydrolyzing peptide bonds. The strategy for each type of metalloprotease begins with generating a nucleophile that attacks the peptide bond that attacks the peptide carbonyl group. O Macmillan Learning On the basis of the information provided in the figure, show the next step in the mechanism for peptide-bond cleavage by a metalloprotease. Metalloproteases H R₁ HN Zn Enz 2+ R₂ Draw curved arrows on the pre-drawn structures to show the metalloprotease mechanism. If you need to reset the structures, click More followed by Reset Drawing. Select Draw Templates Groups More B - H Enz H H с R1 | : HN O | Zn 2+ B R2 N Zn EraseThe enzyme cytidine deaminase catalyzes the conversion of cytidine to uridine. Cytidine deaminase catalyzes the reaction through an addition of water across the cytidine 3,4-bond, forming a tetrahedral intermediate followed by the elimination of NH3 to form the product uridine. This is like the addition-elimination mechanism that we studied for adenosine deaminase. Cytidine deaminase НО. NH₂ N пOH OH cytosine R + H₂O cytidine The Km value for the substrate cytidine is 2.5 × 10-4 M, and the K; for competitive inhibition by the product uridine is 2.5 × 10-³ M. N R A reduced derivative of the product, 3,4,5,6-tetrahydrouridine was shown to be a fully reversible competitive inhibitor with a Ki of 2.4 x 10-7 M, a value approximately 10,000 times lower than that of the product uridine. NH₂ NH uridine HO. N R R = D-ribose HOH OH uridine 3NH uracil ring numbering H NH H H + NH3 H OH H 3,4,5,6-tetra- hydrouridine a.) Draw a structure of the intermediate that we predict to form during the…In each case, these are enzymes that catalyze thesame reaction in different species. The question is: are they related or not? i.e. Are the structures essentially the same? Often you can get similar reactions from proteins thatevolved from a common ancestor (e.g., trypsin and chymotrypsin). Sometimes the samereaction can be catalyzed by proteins with very different evolutionary origins and with verydifferent structures (e.g., trypsin and subtilisin). Your job is to decide if these proteins have fundamentally different folds or if they have basically the same fold. Briefly justify your answer.1. Aminopeptidases from a mammal (PR1A) and the malaria parasite (PR1B)2. Bisphosphoglycerate mutase from a mammal (PR2A) and the toxoplasma parasite(PR2B)
- In the fungus Neurospora, some mutants were obtainedthat lacked activity for a certain enzyme. The mutationswere found, by mapping, to be in either of two unlinkedgenes. Provide a possible explanation in reference to quaternary protein structure. The following diagram shows the biosynthesis of B12 coenzymes, starting with the vitamin. DMB is dimethylbenzimidazole. (a) What one additional substrate or cofactor is required by enzyme B? (b) Genetic deficiency in animals of enzyme C would result in exces- sive urinary excretion of what compound?When performing his experiments on protein refolding, Christian Anfinsen obtained a quite different result when reduced ribonuclease was reoxidized while it was still in 8 M urea and the preparation was then dialyzed to remove the urea. Ribonuclease reoxidized in this way had only 1% of the enzymatic activity of the native protein. Why were the outcomes so different when reduced ribonuclease was reoxidized in the presence and absence of urea?
- If the substrate for an enzyme catalyzed reaction contained a negative charge, which of the following amino acids would most likely be present in the active site to provide electrostatic destabilization of the ES complex? Leu Val O Asp O LYS QUESTION 15 What is the function of the histidine in the diagram of the mechanism at right with the substrate, a phenylalanine residue? (n) His Asp Nucleophilic affack by water stabilization of a metal ion covalent catalysis electrostatic attraction of the substrate O acid base catalysis 789 Mustly cloudy Click Save and Submit to save and submit. Click Save All Ansuwers to save all answers. here to searchFull length resilin that is not in a cell is thought by some to form a tertiary structure of this form (picture attached) The yellow portions represent exon 1 and the blue portions exon 3. These structures assemble into a kind of lattice or network. In full length resilin, stress in the form of mechanical pressure or heating to remove water results in a tighter network that excludes any water internally. How might this behavior of resilin produce its ‘elasticity’? Explain how the looser water containing structure and the tighter water excluding structure may give us a mechanism for the elasticity.Contrast the resultant orientation of themacrodipoles of cytochrome b562 consisting of 4 alpha-heli-ces with that in bacteriorhodopsin consisting of 7 alpha-heli-ces. The diagram of bacteriorhodopsin on the right takenfrom the textbook (Figure 11-10) shows that the C-termi-nal end of the helix-7 is located in the cytoplasm. Thefunction of this protein is translocate protons from the cy-toplasm to the exterior. How might the terminal -COO-group and the helix dipole of helix #7 augment or dimin-ish the function of the protein?.
- Hydrolysis of the N-glycosyl bond between deoxyribose and a purine in DNA creates an AP site. An AP site generates a thermodynamic destabilization greater than that created by any DNA mismatched base pair. This effect isnot completely understood. Examine the structure of an AP site anddescribe some chemical consequences of base loss.Allosteric Regulation of Ribonucleotide Reductase by ATP and Deoxynucleotides Describe the underlying rationale for the regulatory effects exerted on ribonucleotide reductase by ATP, dATP, dTTP, and dGTP.Match the following nucleobases (designated AD) with their names and answer questions about them. NH, NH, C D NH2 Note that some of the items from the answer list should NOT be used. Guanine 1. Aand B - Cytosine 2 Cand D • Adenine 3. Not shuwn v Thymine 4. D v Uracil 5. B a Aand C v Which of tho shown bases are pyrimidines? 7. A and O v Which of the shown bases form canonical A-T Watson-Crick base pair? S. A v Which of the shown bases form canonical G-C Watson.Crick base-pair? 9. Band C 10. C 11. Band D