Radioactive uracil can be used to label all of the pyrimidine residues in DNA. Using either names or structures, present pathways for the conversion of uracil to dTTP and to dCTP. For each reaction, show the involvement of cofactors, and identify sites of allosteric regulation

Q: Residue Asn 204 in the glucose binding site of hexokinase IV was mutated, in two separate…

A: Enzymes are protein molecules that increase the rate of reaction by decreasing the activation…

Q: if the reaction pH drops significantly (pH=2 for example), how would reaction catalyzed be serine…

A: Serine protease are the enzymes that cleave peptide bonds in proteins in which serine serves as…

Q: Radioactive uracil can be used to label all of the pyrimidine residues inDNA. Using either names or…

A: Allosteric regulation is the regulation of an enzyme by binding an effector molecule at a site other…

Q: If isolated regulatory subunits and catalytic subunits of ATCase are mixed, the native enzyme is…

A: ATcase (Aspartate transcarbamoylase) is an allosteric enzyme. It is involved in regulation of…

Q: Gout is a medical condition usually caused by a deficiency of the salvage enzyme…

A: Introduction: Allopurinol is the first choice of drug in the condition of chronic gout (long-term…

Q: Which of the following amino acid residues would not provide a side chain for acid-base catalysis at…

A: Amino acids are the building blocks of proteins, which are essential to the structure and function…

Q: Identify the most cost effective enzyme purification method and provide brief explanations for this…

A: Enzymes need to be purified from cell extract to remove the undesired compounds which helps to…

Q: Page 3 2) 7. J a) Glucosidase I catalyzes hydrolysis of specific glucosidase I is a synthetic…

A: Parameters such as Km and vmax are used for comparing enzyme activities. If we know the initial rate…

Q: The enzyme lysozome catalysis the hydrolysis of polymer that consists of N-acetylglucosamine and…

A: Lysozyme is found in the secretions like tears, and sweat. It cleaves the beta 1-4 glycosidic bond…

Q: Phosphoglycerate kinase shows induced fit resulting from the binding of both substrates to form the…

A: Phosphoglycerate kinase is a glycolysis enzyme that catalyses the seventh reaction in the ten-step…

Q: What features distinguish enzymes that undergo allosteric control from those that obey…

A: Enzyme are the catalysts which increase the rate of reactions without affecting the equilibrium of…

Q: If the substrate for an enzyme catalyzed reaction contained a negative charge, which of the…

A: We are authorized to answer one question at a time since you have not mentioned which question you…

Q: 3CLpro is a cysteine protease, which are among the most common proteases in biochemistry, however…

A: The 3 dimensional conformation of a biomolecule is highly specific and vital to its function,…

Q: Radioactive uracil can be used to label all of the pyrimidine residues in DNA. Using either names or…

A: Deoxyribonucleic acid is a molecule composed of two polynucleotide chains that coil around each…

Q: The protein catalase catalyzes the reaction 2 H,O,(aq) — 2 H₂O(1) + O₂(g) S and has a…

A: Reaction: 2H₂O₂(aq) → 2H2O(l) + O2(g)Km = 25 mMTurnover number Kcat =  4.0 × 107s–1Total enzyme…

Q: a) Based on the mechanism shown in Figure 2A, what type of enzyme is transpeptidase? : Lyase…

A: Note : Hi ! Thank you for the question. We are authorized to answer three subparts at a time. Since…

Q: Given the following reaction, identify the class and subclass of the enzyme involved. CH2OH C=O…

A: Enzymes catalyse the reaction either by making or breaking the bond. They might form double bonds or…

Q: Comment on Figure 2a and Figure 2b regarding stabilization of the transition state and…

A: From the given energy diagrams; It is seen that the enzyme (E) and the substrate (S) at the start of…

Q: Draw the structure of PTH-derivative that is formed after Fpg is subjected to one cycle of Edman…

A: Draw the Structure of PTH which is formed when  react with Edman degradation?

Q: Chymptrysin preferentially binds thetransition state. Explain what is meant by this.

A: Chymotrypsin is defined as a “hydrolytic enzyme”. It is a member of the super-family, belonging to…

Q: Draw a mechanism using the general features of a serine protease to explain how inhibitor x might…

A: Inhibitors can be broadly classified into reversible and irreversible inhibitors. If the bond…

Q: Based on our class discussion of the currently accepted mechanism for ribosome catalysis, draw a…

A: By transferring the nascent peptide chain from P-site peptidyl-tRNA to A-site aminoacyl-tRNA…

Q: Provide an example of covalent catalysis in the mechanism of chymotrypsin. What is the nucleophile…

A: Chymotrypsin is a digestive enzyme that hydrolyzes peptide bonds, specifically at the carboxyl side…

Q: Define what lectins are and outline their biochemical functions.

A: Carbohydrate binding proteins (CBP) are the proteins that can interact with sugar chains but do not…

Q: Describe a common feature at the active site of serine proteases and acetyl cholinesterase

A: Acetylcholinesterase is an enzyme that catalyzes the hydrolysis of acetylcholine (which is a…

Q: The objective is to study a novel protease P isolated from the digestive tract of an Amazonian…

A: SDS-PAGE: Sodium Dodecyl Sulphate-Polyacrylamide Gel Electrophoresis (SDS PAGE) is a method for…

Q: under certain conditions alpha helical bundles can form and can facilitate protein insertion into…

A: Integral membrane proteins fold into their active conformations in a complex milieu dictated by the…

Q: Describe type I, II, and III L-asparaginases. Mention characteristics and differences between them…

A: L-Asparaginase Enzymes having antitumor activities. Degrade asparagine to aspartate with the…

Q: From the complete oxidation of glucose (glucose  →  6CO2), how many total nucleotide triphosphates…

A:

Q: RuBP carboxylaseis by no means an idesl enzyme. Describe some of the problems with its active site…

A: The process of photosynthesis involves two phases – photochemical phase and biosynthetic phase. In…

Q: Construct the mechanism of a serine-protease with a catalytic triad.

A: A serine protease is an enzyme that cleaves peptide bonds in proteins and peptides. It possesses a…

Q: OBJECTIVES To compute the nutritional value of hypothetical food product To…

A: Nutritional value of a food product is the percentage or amount of different components present in…

Q: Lysozyme is a catalytic enzyme that cleaves NAG-NAM units in the bacte- rial cell wall, and is found…

A: Lysozyme is a naturally occurring enzyme found in secretions such as tears, saliva and milk. It…

Q: From the complete oxidation of glucose (glucose  →  6CO2), how many total nucleotide triphosphates…

A: Glucose metabolism's major pathway is glycolysis. Which take place in both aerobic…

Q: Which strategies listed does this enzyme use to facilitate cleavage of α-galactoside? Choice 1 of…

A: Alpha-galactosidase enzymes are homodimeric glycoprotein which catalyzes the cleavage of terminal…

Q: What role do low-barrier hydrogen bonds play in serine protease catalysis?

A: A low barrier hydrogen bond is a special type of hydrogen bond which can occur when the pKa of the…

Q: What cofactors are necessary for methyltransferases t Homocysteine Methionine o work?

A: Methyltransferases are primarily responsible for the transfer of methyl groups to other molecules.

Q: 1. Please fully explain (use illustrate where appropriate) the Modes of Enzyme Catalysis exemplified…

A: The active site of chymotrypsin consist of a combination of 3 specific amino acid residues that work…

Q: What are the measures to inhibit the Maillard reaction in undesirable situations. please explain…

A: Maillard reaction is a type of chemical reaction in the field of Biochemistry. It occurs between a…

Metabolic pathways

Metabolism is defined as the group of life-supporting, enzyme-mediated chemical reactions in organisms. A metabolic pathway is a set of these chemical reactions that involve anabolism (synthesis of complex biomolecules) and catabolism (breakdown of biomolecules into small molecules) that occur inside a cell. Metabolites are the reacting substances, products, and intermediate substances of an enzymatic process that are altered by a series of chemical events catalyzed by enzymes.