Identify factors that account for the high phosphoryl-transfer potential of the nucleoside triphosphates, NTPs. charge repulsion increase in entropy decrease in entropy stabilization by hydration low standard free energy of hydrolysis
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- Diagram the hydrogen-bonding interactions of the catalytic triad His–Lys–Ser during catalysis in a hypothetical hydrolytic enzyme.The reaction catalyzed by phosphorylase is readily reversible in vitro. At pH 6.8, the equilibrium ratio of orthophosphate to glucose 1-phosphate is 3.6. The value of ΔG°’ for this reaction is small because a glycosidic bond is replaced by a phosphoryl ester bond that has a nearly equal transfer potential. However, phosphorolysis proceeds far in the direction of glycogen breakdown in vivo. Suggest one means by which the reaction can be made irreversible in vivo.Intramitochondrial ATP concentrations are about 5 mM, and phosphate concentration is about 10 mM. If ADP is five times more abundant than AMP, calculate the molar concentrations of ADP and AMP at an energy charge of 0.85. Calculate AG for ATP hydrolysis at 37 °C under these condi- tions. The energy charge is the concentration of ATP plus half the concen- tration of ADP divided by the total adenine nucleotide concentration: [ATP] + 1/2[ADP] [ATP] + [ADP] + [AMP]
- Identify each reaction catalyzed by (a) a nucdeotidase; (b) a phosphorylase; (c) a phosphoribosyltransferase. GMP A D E Guanine Guanosine FHis388 Glu357 His388 Glu357 Ring opening Proton HO HO abstraction HO но- G6P He NH- NH His388 His388 His388 Glu357 Glu357 Glu357 HO но HO но- но OH cis-enediol F6P Ring closure intermediate OH 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.Intramitochondrial ATP concentrations are about 5 mM, and phos- phate concentration is about 10 mM. If ADP is five times more abundant than AMP, calculate the molar concentrations of ADP and AMP at an energy charge of 0.85. Calculate AG for ATP hydrolysis at 37 °C under these conditions. The energy charge is the concentra- tion of ATP plus half the concentration of ADP divided by the total adenine nucleotide concentration: [ATP] + 1/2[ADP] [ATP] + [ADP] + [AMP]
- From the complete oxidation of glucose (glucose 6CO2), how many total nucleotide triphosphates are yielded (be sure to deduct payback) as part of substrate level phosphorylation? 灣Lysozyme is a catalytic enzyme that cleaves NAG-NAM units in the bacte- rial cell wall, and is found in external secretions of the body. Why does thisWhen free water molecules are excluded from an enzyme’scatalytic pocket, is a catalytic —OH group a stronger orweaker nucleophile? Explain.
- calculate the turnover number for an enzyme, assuming Vmax is 0.5M.sec-1 and the concentration of the enzyme used is 0.002M . why is it usefull to know this?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.Intramitochondrial ATP concentrations are about 5 mM, and phosphate concentration is about 10 mM. If ADP is five times more abundant than AMP,calculate the molar concentrations of ADP and AMP at an energy charge of 0.85. Calculate ∆G for ATP hydrolysis at 37 °C under these conditions.The energy charge is the concentration of ATP plus half the concentration of ADP divided by the total adenine nucleotide concentration.