5) The disease Phenylketonuria (or PKU) occurs when the enzyme that helps to catalyze the conversion of the amino acid phenylalanine into non-harmful tyrosine is mutated and doesn't work as well (or at all). Phenylalanine will still break down into tyrosine by itself, because this is a favorable reaction. Why is the non-functional enzyme a problem? Explain in a few sentences.
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- Histidine is frequently used as a general acid or base in enzyme catalysis. Considering the pKa value of the side chain, suggest a reason why is this so?. 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?A carboxypeptidase is a metalloenyme (its active site contains one or more metal ions essential for the function) that catalyzes the hydrolysis of the peptide bond of the terminal amino acid of a polypeptide chain (where the free carboxyl group occurs). The binding of an L-alanyl-L-tyrosine peptide substrate in the active site of the enzyme is represented in the scheme below: Glu Zn++ COO™ OH H3C CH₂ HC NH IO C H H Poche apolaire -H H O+N: C N H H H NH₂ Arg 145 Туг 248 NB: This scheme gives a planar representation of the spatial structure of the active site where indicated contacts (hatched lines) are supposed to occur in the 3D structure of the enzyme. 1- Describe the interactions that occur between the ligand and amino acid residues of the active site. 2- What would be the impact on the Km value if we replace L-alanyl-L-tyrosine by the following substrates: L-alanyl-L-phenylalanine; L-alanyl-L-aspartate; L-aspartyl-L- tyrosine.
- The hexokinases are a class of enzymes that catalyze the ATP-dependent phosphorylation of hexoses (sugars with six carbons). The hexokinases will bind only D-hexose sugars and not their L-counterparts. In general terms, describe the features of enzyme structure that make this specificity possible.The compound below, doxorubicin, is a substrate for p-glycoprotein. Cancer cells with a higher expression of P-gp (more P-gp protein per cell) than normal cells were treated with doxorubicin. What would be the expected observation? o= 0= OH O OH HCI OH -OH NH₂ & OH more doxorubicin inside the cell doxorubicin would be oxidized doxorubicin would have more cytotoxic effect on these cancer cells less doxorubicin inside the cellWhen 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?
- The enzyme hexokinase adds a phosphate toD-glucose but ignores its mirror image, L-glucose. Supposethat you were able to synthesize hexokinase entirely fromD-amino acids, which are the mirror image of the normalL-amino acids.A. Assuming that the “D” enzyme would fold to a sta-ble conformation, what relationship would you expect it tobear to the normal “L” enzyme?B. Do you suppose the “D” enzyme would add aphosphate to L-glucose, and ignore D-glucose?The enzyme ATCase (Aspartate TransCarbamoylase) catalyzes an early step in the synthesis of the pyrimidine nucleotides. The activities of the ATCase reactions are shown in the following plots. Which one of the following statements is most correct description about this enzyme and/or this enzyme-catalyzed reaction? ATP No allosteric effectors Vo CTP ATCase 10 20 30 40 (Aspartate] (mM) O A. This enzyme is allosterically inhibited by ATP. B. This enzyme is composed of multiple subunits. C. "ATP" binds to catalytic subunits of ATCase. O D."CTP" binds to the R-state enzyme. O E. At high concentrations of ATP, ATP binds to the T-state enzyme, thus increase the affinity for the substrate [S].1)Catalase a. Is catalase activity endothermic or exothermic? b. What classification of enzyme is catalase? c. Give the Enzyme Commission (E.C.) number of catalase. d. Is catalase reusable? answer all and don't copy from other sources I will downvote for sure
- Triosephosphate isomerase (TIM) catalyzes the conversion of dihydroxyacetone phosphate to glyceraldehyde-3-phosphate. The enzyme’s catalytic groups are Glu 165 and His 95. In the first step of the reaction, these catalytic groups function as a general-base and a general-acid catalyst, respectively. Propose a mechanism for the reaction.In a bisubstrate reaction, a small amount of the fi rst product P is isotopically labeled (P*) and added to the enzyme and the fi rst substrate A. No B or Q is present. Will A (= P—X) become isotopically labeled (A*) if the reaction follows a Sequential mechanism?Snake venom contains many hydrolase enzymes, including several serine proteases. One such protease (present in high concentrations in snake venom) mimics the action of thrombin to activate fibrin. The venom protease cleaves peptide bonds with a specificity for basic, positively charged amino acids. This enzyme is incubated with a substrate peptide with the sequence SNPDCKVALYMTW. Draw a mechanism for the peptide hydrolysis of this specific peptide catalyzed by this snake venom protease. Include the structure of the active site amino acids of the enzyme and the substrate peptide group (including the full structure of the 2 specific amino acids that contribute to the scissile peptide group in the substrate) in your mechanism. Use the curved arrow convention to illustrate the flow of electrons.