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Questions and Answers
What function do ligases perform in enzymatic reactions?
What function do ligases perform in enzymatic reactions?
- They catalyze the hydrolysis of proteins.
- They assist in moving molecules across membranes.
- They bind to the enzyme-substrate complex only.
- They utilize ATP to form bonds between large molecules. (correct)
Which type of enzyme inhibition results in a permanent loss of activity?
Which type of enzyme inhibition results in a permanent loss of activity?
- Uncompetitive inhibition
- Competitive inhibition
- Irreversible inhibition (correct)
- Non-competitive inhibition
What does the Michaelis constant (K_m) indicate in enzyme kinetics?
What does the Michaelis constant (K_m) indicate in enzyme kinetics?
- The substrate concentration required for half maximal enzyme activity. (correct)
- The pH level at which enzyme activity is optimal.
- The maximum reaction rate when the enzyme is saturated.
- The affinity of an inhibitor for the enzyme.
What role does chymotrypsin play in biological processes?
What role does chymotrypsin play in biological processes?
Which type of enzyme assists in moving molecules across membranes?
Which type of enzyme assists in moving molecules across membranes?
What is the main role of enzymes in chemical reactions?
What is the main role of enzymes in chemical reactions?
What does the induced fit model explain about enzyme function?
What does the induced fit model explain about enzyme function?
Which factor can lead to enzyme denaturation?
Which factor can lead to enzyme denaturation?
What component is referred to as an apoenzyme?
What component is referred to as an apoenzyme?
Which of the following is a function of oxidoreductases?
Which of the following is a function of oxidoreductases?
What class of enzymes catalyze the transfer of specific functional groups?
What class of enzymes catalyze the transfer of specific functional groups?
What is the function of cofactors in enzyme activity?
What is the function of cofactors in enzyme activity?
What distinguishes lyases from other enzyme classes?
What distinguishes lyases from other enzyme classes?
Flashcards
Enzyme Kinetics Vmax
Enzyme Kinetics Vmax
Maximum reaction rate of an enzyme when saturated with substrate.
Enzyme Kinetics Km
Enzyme Kinetics Km
Substrate concentration at half of maximum reaction rate; measures enzyme-substrate affinity.
Enzyme Inhibition Types
Enzyme Inhibition Types
Different ways an inhibitor reduces/stops enzyme activity by binding to the enzyme.
Ligase's Role
Ligase's Role
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Enzyme 3D structure
Enzyme 3D structure
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Enzyme function
Enzyme function
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Induced fit model
Induced fit model
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Enzyme inhibition
Enzyme inhibition
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Enzyme catalysis
Enzyme catalysis
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Oxidoreductases
Oxidoreductases
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Hydrolases
Hydrolases
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Enzyme factors
Enzyme factors
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Study Notes
Enzymes
- Enzymes are biological catalysts that speed up chemical reactions
- They lower the activation energy, making reactions easier to occur
- Enzymes are typically globular proteins, soluble in water, and highly specific in their activity, which is dictated by their structure
- Induced fit model:
- The active site is not a perfect match for the substrate initially.
- The substrate binding to the active site induces a conformational change in the enzyme, creating a better fit.
- This better fit lowers the activation energy.
Key Factors Affecting Enzyme Function
- Temperature: Enzymes can be denatured at extreme temperatures.
- pH: Enzymes can be denatured by extreme pH values.
- Inhibition: Cofactors and coenzymes play significant roles, influencing enzyme function.
- Apoenzyme: the protein component without its cofactor.
- Coenzymes: organic cofactors.
- Inorganic cofactors: cations like Zn2+, Mg2+, etc.
- Covalent catalysis: temporary covalent bonds between enzymes and substrates form an acyl-enzyme intermediate, crucial for catalysis
Enzyme Classes
- Enzymes are categorized into 7 classes
- Oxidoreductases
- Transferases
- Hydrolases
- Lyases
- Isomerases
- Ligases
- Translocases
Enzyme Nomenclature
- Enzymes have a 4-part number, starting with 'EC', e.g., EC 2.7.7.7 -Enzyme class -Serial (ID) number -Subclass -Sub-subclass (substrate)
Enzymes Kinetics
- Vmax: the maximum rate of an enzyme-catalyzed reaction when the enzyme is fully saturated with substrate
- Km: the substrate concentration at which the reaction rate is half of Vmax. It reflects the enzyme's affinity for the substrate. A lower Km indicates higher affinity
Enzyme Inhibition
- Competitive inhibition: inhibitor binds to the active site, preventing substrate binding.
- Non-competitive inhibition: inhibitor binds to a site other than the active site, changing the enzyme's shape and reducing its activity.
- Uncompetitive inhibition: inhibitor binds only to the enzyme-substrate complex, preventing further reaction and decreasing Vmax and Km.
- Mixed inhibition: inhibitor binds to the enzyme at either the active site or a different site, altering Vmax and Km.
- Irreversible inhibition: inhibitor forms a covalent bond with the enzyme, permanently inactivating it , reducing Vmax
Enzyme Structure and Function
- Tertiary structure: is responsible for the 3-D shape of enzymes.
- Bonds in enzyme structure: Hydrogen bonds, disulfide bonds, peptide bonds, and ionic bonds contribute significantly
- Factors affecting enzyme activity: pH, substrate concentration, temperature, and enzyme concentration.
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