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Questions and Answers
What is the primary function of thrombin in the blood clotting process?
What is the primary function of thrombin in the blood clotting process?
Which of the following describes the physical characteristics of plasma?
Which of the following describes the physical characteristics of plasma?
Where are plasma-specific enzymes primarily secreted?
Where are plasma-specific enzymes primarily secreted?
In which system does thrombin primarily exert its action?
In which system does thrombin primarily exert its action?
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What role do plasma-specific enzymes play in the bloodstream?
What role do plasma-specific enzymes play in the bloodstream?
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What defines the active site of an enzyme?
What defines the active site of an enzyme?
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What is the role of a coenzyme in the context of an apoenzyme?
What is the role of a coenzyme in the context of an apoenzyme?
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Which component forms a holoenzyme?
Which component forms a holoenzyme?
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What is a substrate?
What is a substrate?
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What characterizes allosteric sites in enzymes?
What characterizes allosteric sites in enzymes?
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What happens during the transition state of an enzyme-catalyzed reaction?
What happens during the transition state of an enzyme-catalyzed reaction?
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What is a common feature of metalloenzymes?
What is a common feature of metalloenzymes?
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Which option best describes primary structure in the context of enzymes?
Which option best describes primary structure in the context of enzymes?
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What is the primary significance of CK-MB in medical diagnostics?
What is the primary significance of CK-MB in medical diagnostics?
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Which classification of enzyme names is characterized by being not specific and based on organic observation?
Which classification of enzyme names is characterized by being not specific and based on organic observation?
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What role does electrophoresis play in the study of isoenzymes?
What role does electrophoresis play in the study of isoenzymes?
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Which enzyme is not considered as an arbitrary name classification?
Which enzyme is not considered as an arbitrary name classification?
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Which of the following statements about isoenzymes is true?
Which of the following statements about isoenzymes is true?
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Which enzyme listed is primarily involved in protein digestion?
Which enzyme listed is primarily involved in protein digestion?
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What does the term 'bilocular' refer to in the context provided?
What does the term 'bilocular' refer to in the context provided?
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Which characteristic distinguishes CK-MB from CK-MM?
Which characteristic distinguishes CK-MB from CK-MM?
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What suffix is typically added to the name of enzymes based on the substrate or group they act upon?
What suffix is typically added to the name of enzymes based on the substrate or group they act upon?
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Which enzyme class is primarily responsible for transferring intact groups of atoms like amine or phosphate from one substrate to another?
Which enzyme class is primarily responsible for transferring intact groups of atoms like amine or phosphate from one substrate to another?
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Which enzyme is classified as a hydrolase that catalyzes the hydrolysis of various bonds with the presence of water?
Which enzyme is classified as a hydrolase that catalyzes the hydrolysis of various bonds with the presence of water?
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Which of the following enzymes catalyzes the removal of groups from substrates without hydrolysis?
Which of the following enzymes catalyzes the removal of groups from substrates without hydrolysis?
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What is the function of aldolase in the context of enzyme classification?
What is the function of aldolase in the context of enzyme classification?
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Which enzyme is specifically mentioned as an inhibitor for ACP in plasma?
Which enzyme is specifically mentioned as an inhibitor for ACP in plasma?
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Which of the following enzymes is NOT categorized under hydrolases?
Which of the following enzymes is NOT categorized under hydrolases?
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Which enzyme catalyzes the conversion of starch into glucose?
Which enzyme catalyzes the conversion of starch into glucose?
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Which classification of enzyme is primarily responsible for catalyzing oxidation and reduction reactions?
Which classification of enzyme is primarily responsible for catalyzing oxidation and reduction reactions?
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According to the lock and key theory, what is essential for the enzyme and substrate interaction?
According to the lock and key theory, what is essential for the enzyme and substrate interaction?
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What does the induced fit theory suggest about enzyme-substrate interaction?
What does the induced fit theory suggest about enzyme-substrate interaction?
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Which factor does NOT influence the binding of enzymes to substrates?
Which factor does NOT influence the binding of enzymes to substrates?
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Which enzyme classification is best associated with the assessment of liver problems?
Which enzyme classification is best associated with the assessment of liver problems?
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Study Notes
Active Site
- The specific region on an enzyme where the substrate binds, forming an enzyme-substrate complex.
- Both binding and catalytic reactions occur at the active site.
Substrate
- The substance acted on by an enzyme.
Product
- The substance derived from a transformed substrate (enzyme + substrate).
Allosteric Site
- A cavity on the enzyme, separate from the active site, that can bind regulatory molecules.
- This site influences the enzyme's structure and function.
Apoenzyme
- The enzyme portion that cannot function alone, requiring a coenzyme.
Holoenzyme
- The complete enzyme complex composed of an apoenzyme and a coenzyme.
Metalloenzyme
- An enzyme that contains an inorganic activator as part of its molecular structure.
Primary Structure
- The specific amino acid sequence of an enzyme.
Enzyme Variants
- Heteroenzyme: Enzymes with the same enzymatic activity but specific to different biological species (e.g., Lactate dehydrogenase (LDH) of rabbits and humans).
- Plasma-Specific Enzymes: Enzymes secreted by the liver and released into the plasma. They contribute to plasma function (e.g., blood clotting, fibrinolytic system).
- Bilocular: Enzymes released by mitochondria and cell sap.
Isoenzymes
- Multiple forms of an enzyme that catalyze the same reaction but have slightly different structures and properties.
- CK-MB: A sub-unit of creatine kinase (CK) important for heart and skeletal muscle function. More specific and sensitive than CK-MM. Used in diagnosing acute myocardial infarction, particularly within the first 12 hours.
Characteristics of Isoenzymes
- Electrophoresis: Used to classify isoenzyme sub-units based on their charge and mobility.
- Response to Activation and Inactivation: Isoenzymes respond differently to activation and inactivation processes (e.g., formaldehyde activation of ACP-RBC and inactivation of ACP-Prostate).
- Response to Inhibitors: Plasma enzymes are susceptible to inhibitors. Various substances like fluoride, heparin, or oxalic acid can inhibit ACP activity.
Nomenclature and Classifications of Enzymes
Empirical Names
- Not specific, based on organ, observation, experiences, or the type of chemical reaction.
- Arbitrary: Not specific (e.g., Ptyalin, Trypsin, Pepsin, Rennin).
- Suffix -ase: Added to the name of the substrate or group acted upon by the enzyme to describe the catalyzed reaction (e.g., Maltase).
Classifications of Enzymes
- Oxidoreductase: Catalyze oxidation (addition of H ion) and reduction reactions (removal of H ion) between two substances (e.g., Oxidases, Dehydrogenases).
- Transferase: Catalyze the transfer of an intact group of atoms (amine or phosphate group) from one substrate to another (e.g., Aminotransferase, Kinase, Phosphorylase, Methyltransferase).
- Hydrolases: Catalyze hydrolysis of various bonds, requiring water for the reaction to proceed (e.g., Phosphatase, Phosphodiesterase, Protease).
- Lyases: Catalyze the removal of groups from substrates without hydrolysis. This leads to double bonds (e.g., Decarboxylase).
Factors Affecting Enzyme Binding
- Energy: Activation energy required for a reaction.
- Molecular Compatibility: The similarity between the enzyme and substrate.
- Space Availability: The number of enzymes and substrates available for reaction.
- Specificity: The enzyme's ability to catalyze a specific substrate.
Specificity of Enzyme Action
- Lock and Key Theory: Proposed by Emil Fischer. The active site of the enzyme is always complementary to the substrate, ensuring recognition between the two.
- Induced Fit Theory: Proposed by Daniel Koshland. The enzyme modifies its shape upon substrate binding, ensuring complementarity between the two only after binding.
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Description
Explore the fundamental concepts related to enzyme structure, including active sites, substrates, and types of enzymes. Understand how different sites and structures, such as allosteric and holoenzymes, influence enzymatic activity. This quiz will deepen your knowledge of biochemistry and enzyme functionality.
