Enzyme Lecture 12: ENZYMES

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18 Questions

What is the main reason an active site is compatible with its substrate?

It has a shape compatible with the substrate

Which residues are directly involved in the making and breaking of bonds within the substrate?

Catalytic groups

What happens to the catalytic groups after the catalysis is complete?

They go back to their original state

In allosteric modulation, what effect does a positive modulator have on enzyme activity?

Increases activity

What type of enzyme has the same active site and allosteric site?

Homotropic enzyme

In feedback inhibition, which component inhibits the regulatory enzyme?

End product of the pathway

What is the main function of an enzyme?

Catalyze the conversion of substrates into products

Which of the following is a characteristic of enzymes?

Changes the state of the molecule

What does it mean when it is said that enzymes are stereospecific?

They convert only a specific form of a compound

What type of regulation involves the inhibition of an enzyme by the end product of a reaction?

Heterotropic allosteric regulation

Which part of the enzyme is responsible for substrate binding and catalysis?

Active site

In enzyme activity, which mechanism involves the addition of groups like phosphoryl and adenylyl to specific amino acids of proteins to make the enzyme more active?

Covalent modification

What is the term for an inactive enzyme precursor that is activated through proteolytic cleavage by a separate enzyme?

Zymogen

What is the function of a cofactor in enzyme activity?

Assists the enzyme in its function

Why is it important for enzymes to be highly specific in substrate recognition?

To prevent side reactions

Which part of an enzyme is responsible for interacting with the substrate to catalyze a reaction?

Active site

What is the term for the process where some enzymes are produced as inactive precursors and activated through cleavage by proteolytic enzymes to regulate their activity?

Proteolytic cleavage

What type of regulation involves altering enzyme activity through the binding of molecules at a site other than the active site?

Heterotropic allosteric regulation

Explore the characteristics of enzymes, including their role as catalysts, their specificity, and their ability to speed up reactions without being consumed. Learn about examples such as Hexokinase catalyzing the conversion of glucose to glucose-6-phosphate.

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