His388 Glu357 His388 Glu357 Ring opening Proton HO HO abstraction HO G6P His388 Glu357 His388 His388 Glu357 Glu357 HO HO OH ci-enediol intermediate F6P Ring closare Describe the mechanism shown above for phosphoglucose isomerase. • Describe the chemistry of each step · How the enzyme appears or might facilitate the chemistry • How the enzyme increases the reaction rate.

Q: Why was it necessary to use phosphoaminophosphonic acid-adenylate ester (ANP) in the ATP synthase…

A: As per the chemiosmotic Model, ATP synthase is the enzyme that phosphorylates ADP with Pi as…

Q: 33. Which of the following statements is true for the shown reaction? P-D-CH₂ P-D-CH₂ CH₂OH OH A O…

A: 33. Molecule A is fructose-6-phosphate and molecule B is fructose-2,6-bisphospate and its conversion…

Q: R 20 O- protein N CH3 H₂N asparagine side chain HO OH OH activated sugar Draw the product of the…

A: An O-glycosidic bond is a covalent bond formed between a carbohydrate's anomeric carbon and the…

Q: 6F. What conformational state is stabilized by y in ATP synthase? Why might achieving this state…

A: The ATP synthase is a compound found in mitochondrial, restricted in the inward layer, where it aids…

Q: Put the steps of the chymotrypsin's enzymatic reaction in order of events from #1-10. -Tetrahedral…

A: Chymotrypsin is a serine protease enzyme that catalyzes the hydrolysis of specific peptide bonds in…

Q: Match the specificity pocket (identified by red number) to the residue that occupies it. 1 3 4 2 1.…

A: Proteases preferentially hydrolyze polypeptide substrate peptide bonds based on the amino acids…

Q: Given, isas ri Glucose + Pi→ Glucose-6-P ATP + H₂O → ADP + Pi Determine K 'eq for a coupled reaction…

A: Consider a reaction ; A  B. Its biochemical equilibrium constant (K'eq 1) will be;Now consider a…

Q: With a AGO'of -16.7 kJ/mol, the reaction catalyzed by hexokinase is considered to be at equilibrium…

A: Standard free energy change indicates the portion of the total energy of a system that is…

Q: The aspartate carbamoylase (ATCase) is an enzyme that catalyzes the reaction below utilizing the…

A: The scientific name for ATCase is aspartate transcarbamoylase. The enzyme is multimeric. It is made…

Q: Velocity, activity units/mg protein 51 3 2 0 5 15 20 Aspartate concentration, mM - 10 Control With…

A: Enzymes that are under allosteric control can be categorized into two groups;K-series enzymes :…

Q: Look at the synthesis of citryl CoA by citrate synthase in the figure.  Which of the 4 general…

A: Citrate synthase is an important enzyme in citric acid cycle that catalyses the conversion of oxalo…

Q: Catalane in un enzyme that speeds up the decomposition ot hydrogen peroxide H0) to waler and axvgen.…

A: Enzymes are biocatalyst which binds to the substrate and stabilizes the high energy transition state…

Q: 31. The velocity of a particular enzyme-catalyzed reaction varied with pH as shown in the adjacent…

A: Enzyme activity is at its maximum value at the optimum pH. As the pH value is increased above or…

Q: Please draw all of the structures of the intermediates and names of all reactants, intermediates and…

A: Glycolysis is the metabolic pathway that stepwise oxidises glucose to pyruvate to produce ATP and…

Q: Draw me the inhibition reaction mechanism of Cysteine Protease Inhibitor (E64). How the epoxide ring…

A: E64 is a cysteine protease inhibitor. Cysteine proteases are enzymes that have a cysteine residue at…

Q: 4. Describe the role of His in the catalytic mechanism shown.

A: Enzymes are highly specialized proteins that have extraordinary catalytic power, greater than that…

Q: Which of the following intermolecular force is the strongest? London force Dipole-dipole force lonic…

A: Q.1 AnswerThe strongest intermolecular force among the options listed is E) Hydrogen bond.Hydrogen…

Q: The value of kcat for N-Ac-Phe-OC₂H5 is two-fold greater than that for the L-tryptophanyl analog and…

A: Chymotrypsin catalyzed peptide bond hydrolysis takes place in 2 phases after the enzyme binds the…

Q: 11. Quantitative Relationships between Rate Constants to Calculate K, Kinetic Efficiency (kcat/Km)…

A: Kinetic parameters are Km and  Vmax. They are used to determine the efficiency of an enzyme. Km is…