Describe glucose oxidase's substrate, the substrate’s biological relevance, and identify the main interaction that governs how the substrate binds (e.g. specific salt bridges, negative/positive patches, hydrophobic pockets)
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Describe glucose oxidase's substrate, the substrate’s biological relevance, and identify the main interaction that governs how the substrate binds (e.g. specific salt bridges, negative/positive patches, hydrophobic pockets)
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- Describe the key characteristics of oxidative phosphorylation and substrate level phosphorylation.Describe the rate of enzyme-catalyzed reaction with increasing substrate concentration at constant enzyme concentration. In what ways does hydrogen ion concentration affect enzyme activity?distinguish between phosphorylation at the substrate level and oxidative phosphorylation. What do they have in common and where is each performed
- Explain the mechanism by whicha single substrate reaction catalyzed by an enzyme with a single binding sitefor the substrate is able to exhibit sigmoidal kinetics.Discuss how enzyme, together with its cofactors/ coenzymes, interact with its substrate. How do these interactions effect enzyme activity?Explain the mechanism by whicha single substrate reaction catalyzed by an enzyme with a single binding site for the substrate is able to exhibit sigmoidal kinetics.
- Using glucose metabolism, justify the following statement: Metabolic pathways are highly interdependent and are exquisitely controlled by enzyme activity levels and substrate bioavailability.assume that for an enzyme immobilized on the surface of a nonporous support material, the external mass-transfer resisitance for substrate is not negligible as compared to the reaction rate.The enzyme is subject to substrate inhibition are multiple states possible?why or why not? could the effectiveness factor be greater than one?Please explain how the catabolism of ATP supports the anabolism of protein.
- In _____________ inhibition, the EI complex readily dissociates and the enzyme is again available for substrate binding.Explain the major difference between substrate-level phosphorylation and oxidative phosphorylation.Using enzyme kinetics, illustrate the cooperative behavior of allosteric enzymes (plot of reaction velocity versus substrate concentration for instance)
