C1.1 Flashcards
Define catalyst.
State the role of enzymes in the chemical reactions on which life is based.
State that enzymes speed up chemical reactions without being altered, so can be reused.
Define metabolism.
Define specificity in relation to enzyme structure and function.
Outline how control of metabolism is regulated by enzymes.
Contrast anabolic and catabolic reactions.
List three examples of anabolic processes.
List three examples of catabolic processes.
Outline properties of globular proteins.
Explain the relationship between enzyme structure and enzyme specificity, including the structure and function of the active site.
Outline the stages of enzyme catalysis of a chemical reaction.
Describe the induced fit model of enzyme binding.
Explain the role of random collisions in the binding of the substrate with the enzyme active site.
Compare enzyme and substrate movement involved in reactions that occur in the cytoplasm, with large substrates and with immobilized enzymes.
Discuss variation in specificity of different enzymes.
Define denaturation.
Outline the causes and effects of denaturation on enzyme structure and function.
Explain the effects of temperature, pH and substrate concentration on enzyme structure and function with reference to collision theory, temporary and permanent denaturation.
Draw and interpret graphs showing the effects of temperature, pH and substrate concentration of the activity of enzymes.
Identify the manipulated (independent), responding (dependent) and controlled variation in experiments of enzyme catalyzed reactions.
State the unit for enzyme reaction rate.
State two methods for determining the rate of enzyme reaction rates.
Describe three investigative techniques for measuring the activity of an example enzyme.