12 Questions
What happens when the temperature increases by 10°C according to the text?
The enzyme activity doubles
Which type of inhibitor physically binds to the active site of an enzyme?
Competitive inhibitor
In zero-order kinetics, what happens when the maximum velocity of the reaction is reached?
The rate of reaction remains constant
Which enzyme classification catalyzes intramolecular rearrangement of substrates?
Isomerase
What is the function of coenzymes in enzyme activity?
Are necessary for enzyme activity
Which enzyme converts glucose into glucose phosphate?
Isomerase
What is the role of the active site in an enzyme?
Binding and catalyzing chemical reactions
What defines an isoenzyme?
Its different form based on certain properties
Which factor influences enzymatic reaction velocity by causing a faster reaction?
Optimal pH
What happens to the enzyme concentration and reaction velocity relationship?
Reaction velocity increases with higher enzyme concentration
What is the primary characteristic of zymogen?
Inactive structural form of an enzyme
'Apoenzyme' refers to which part of the enzyme?
Protein portion subject to denaturation
Study Notes
Temperature and Enzyme Activity
- Every 10°C increase in temperature doubles enzyme activity until protein denaturation
Inhibitors
- Competitive inhibitors physically bind to the active site, competing with the substrate, and can be reversed by increasing substrate concentration
- Noncompetitive inhibitors bind to an enzyme at a site other than the active site and may be reversible or irreversible
- Uncompetitive inhibitors bind to the enzyme-substrate complex and cannot be reversed by adding more substrate
Cofactors
- Non-protein molecules necessary for enzyme activity
- Activators: inorganic cofactors such as chloride or magnesium ions
- Coenzymes: organic cofactors such as NAD
Enzyme Kinetics
- First-order kinetics: reaction rate varies directly with substrate concentration with a fixed amount of enzyme
- Zero-order kinetics: reaction rate is not affected by adding more substrate at a certain point, and maximum velocity is reached when the rate of increase in velocity is zero
Enzyme Classification
- Oxidoreductases: catalyze oxidation-reduction reactions
- Transferases: catalyze the transfer of a functional group from one substance to another
- Hydrolases: catalyze hydrolysis of compounds with the introduction of water
- Lyases: catalyze removal of a group without hydrolysis
- Isomerases: catalyze intramolecular rearrangement of substrates, converting one isomer to another
Enzyme Terms
- Active site: where substrates attach and undergo chemical reactions
- Allosteric site: a cavity other than the active site
- Isoenzyme: a different form of a particular enzyme based on certain properties
- Isoform: a result of posttranslational modifications or proenzyme
- Zymogen: a structurally inactive form of an enzyme
- Apoenzyme: a protein portion of an enzyme subject to denaturation and loss of activity
Test your knowledge on enzymes with terms like active site, allosteric site, isoenzyme, and more. Learn about the functions and characteristics of different enzymes and their role in biochemical reactions.
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