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Questions and Answers
What happens when the temperature increases by 10°C according to the text?
What happens when the temperature increases by 10°C according to the text?
- The enzyme activity halves
- The enzyme activity doubles (correct)
- The enzyme activity triples
- The enzyme activity remains constant
Which type of inhibitor physically binds to the active site of an enzyme?
Which type of inhibitor physically binds to the active site of an enzyme?
- Competitive inhibitor (correct)
- Activator
- Noncompetitive inhibitor
- Uncompetitive inhibitor
In zero-order kinetics, what happens when the maximum velocity of the reaction is reached?
In zero-order kinetics, what happens when the maximum velocity of the reaction is reached?
- The rate of reaction becomes zero
- The rate of reaction decreases
- The rate of reaction remains constant (correct)
- The rate of reaction increases exponentially
Which enzyme classification catalyzes intramolecular rearrangement of substrates?
Which enzyme classification catalyzes intramolecular rearrangement of substrates?
What is the function of coenzymes in enzyme activity?
What is the function of coenzymes in enzyme activity?
Which enzyme converts glucose into glucose phosphate?
Which enzyme converts glucose into glucose phosphate?
What is the role of the active site in an enzyme?
What is the role of the active site in an enzyme?
What defines an isoenzyme?
What defines an isoenzyme?
Which factor influences enzymatic reaction velocity by causing a faster reaction?
Which factor influences enzymatic reaction velocity by causing a faster reaction?
What happens to the enzyme concentration and reaction velocity relationship?
What happens to the enzyme concentration and reaction velocity relationship?
What is the primary characteristic of zymogen?
What is the primary characteristic of zymogen?
'Apoenzyme' refers to which part of the enzyme?
'Apoenzyme' refers to which part of the enzyme?
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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
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