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Questions and Answers
What is the role of the active site in enzymatic catalysis?
What is the role of the active site in enzymatic catalysis?
What is the term for a precursor of an enzyme that is inactive?
What is the term for a precursor of an enzyme that is inactive?
What is the unit of measurement for enzymatic activity?
What is the unit of measurement for enzymatic activity?
What is the term for a system of multiple enzymes working together?
What is the term for a system of multiple enzymes working together?
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What is the factor that affects enzymatic activity by increasing the energy barrier of the reaction?
What is the factor that affects enzymatic activity by increasing the energy barrier of the reaction?
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What is Km in enzyme kinetics?
What is Km in enzyme kinetics?
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Which of the following enzymes has a high affinity for its substrate?
Which of the following enzymes has a high affinity for its substrate?
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What is the name of the hypothesis proposed by Fischer to explain enzyme-substrate binding?
What is the name of the hypothesis proposed by Fischer to explain enzyme-substrate binding?
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What is the primary role of catalysts in biological systems?
What is the primary role of catalysts in biological systems?
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What is the classification of enzymes based on?
What is the classification of enzymes based on?
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What is the purpose of enzymes in biological systems?
What is the purpose of enzymes in biological systems?
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What is the name of the organization that develops the classification system for enzymes?
What is the name of the organization that develops the classification system for enzymes?
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What is the reactant in the reaction Glucose-6-phosphate → Fructose-6-phosphate?
What is the reactant in the reaction Glucose-6-phosphate → Fructose-6-phosphate?
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What type of enzyme catalyzes the reaction Fructose-1,6-bisphosphate → Glyceraldehyde-3-phosphate + Dihydroxyacetone phosphate?
What type of enzyme catalyzes the reaction Fructose-1,6-bisphosphate → Glyceraldehyde-3-phosphate + Dihydroxyacetone phosphate?
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What is the primary function of enzymes in metabolic pathways?
What is the primary function of enzymes in metabolic pathways?
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What is the name of the process that involves the breakdown of glucose to produce energy?
What is the name of the process that involves the breakdown of glucose to produce energy?
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What is the product of the reaction glutámico + amoníaco?
What is the product of the reaction glutámico + amoníaco?
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Which enzyme is involved in the reaction Sacarosa → Fructosa + Glucosa?
Which enzyme is involved in the reaction Sacarosa → Fructosa + Glucosa?
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What is the name of the product of the reaction Triacilglicerol →?
What is the name of the product of the reaction Triacilglicerol →?
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Which of the following is a characteristic of Apoenzimas?
Which of the following is a characteristic of Apoenzimas?
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What is the term used to describe enzymes that require a metal ion to be active?
What is the term used to describe enzymes that require a metal ion to be active?
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What is the product of the reaction Lactosa →?
What is the product of the reaction Lactosa →?
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Which enzyme is involved in the reaction Pesinógeno →?
Which enzyme is involved in the reaction Pesinógeno →?
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What is the term used to describe the molecule that is converted to an active enzyme?
What is the term used to describe the molecule that is converted to an active enzyme?
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What is the main characteristic of a suicidal inhibitor?
What is the main characteristic of a suicidal inhibitor?
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What is the effect of a non-competitive inhibitor on the Km of an enzyme?
What is the effect of a non-competitive inhibitor on the Km of an enzyme?
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What is the purpose of enzyme regulation?
What is the purpose of enzyme regulation?
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What is the characteristic of an enzyme cascade?
What is the characteristic of an enzyme cascade?
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What is the definition of an isoenzyme?
What is the definition of an isoenzyme?
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What is the effect of a competitive inhibitor on the enzyme-substrate binding?
What is the effect of a competitive inhibitor on the enzyme-substrate binding?
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What is the purpose of using enzymes in the industry?
What is the purpose of using enzymes in the industry?
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What is the effect of heat on enzyme activity?
What is the effect of heat on enzyme activity?
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What is the diagnosis of Marcelo's symptoms?
What is the diagnosis of Marcelo's symptoms?
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What is the function of the pancreas in digestion?
What is the function of the pancreas in digestion?
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What is the effect of ethanol on pancreatic enzymes?
What is the effect of ethanol on pancreatic enzymes?
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What is the relationship between lithiasis biliar and pancreatitis?
What is the relationship between lithiasis biliar and pancreatitis?
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What is the effect of pancreatitis on pancreatic exocrine secretion?
What is the effect of pancreatitis on pancreatic exocrine secretion?
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What type of enzymes are involved in pancreatic digestion?
What type of enzymes are involved in pancreatic digestion?
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What is the consequence of pancreatitis on the pancreas itself?
What is the consequence of pancreatitis on the pancreas itself?
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What is the dual function of the pancreas?
What is the dual function of the pancreas?
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Study Notes
Enzymes
- Enzymes are biological molecules that accelerate chemical reactions in living organisms.
- They are essential in biological systems as they increase reaction rates, allowing cells to maintain homeostasis and perform various functions.
Classification of Enzymes
- Enzymes can be classified into different groups based on their mode of action and the type of reaction they catalyze.
- Examples of enzyme classes include oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases.
Metabolic Reactions
- Glucose-6-phosphate is converted to fructose-6-phosphate in a reaction catalyzed by an aldose isomerase.
- Fructose 1,6-bisphosphate is converted to glyceraldehyde 3-phosphate and dihydroxyacetone phosphate in a reaction catalyzed by an aldolase.
- Acetylglutamic acid and ammonia are converted to glutamine in a reaction catalyzed by a glutamine synthetase.
- Malate is converted to oxaloacetate in a reaction catalyzed by a malate dehydrogenase.
Pre-metabolic Reactions
- Sucrose is broken down into glucose and fructose in a reaction catalyzed by a sucrase.
- Lactose is broken down into galactose and glucose in a reaction catalyzed by a lactase.
- Triacylglycerol is broken down into β-monoacylglycerol and fatty acid salts in a reaction catalyzed by a lipase.
Activation of Zymogens
- Zymogens are inactive enzyme precursors that require activation to become functional enzymes.
- Examples of zymogens include pepsinogen, trypsinogen, and chymotrypsinogen.
Properties of Enzymes
- Apoenzymes are protein components of enzymes that lack catalytic activity without a cofactor.
- Coenzymes are non-protein molecules that bind to apoenzymes to form active enzymes.
- Examples of coenzymes include NAD+, FAD, and CoA.
Metalloenzymes
- Metalloenzymes are enzymes that contain a metal ion as a cofactor.
- Examples of metalloenzymes include iron-containing enzymes, copper-containing enzymes, zinc-containing enzymes, and magnesium-containing enzymes.
Enzyme Catalysis
- Enzyme catalysis involves the binding of a substrate to an enzyme's active site, followed by a conformational change that facilitates the reaction.
- The enzyme-substrate complex is stabilized by weak bonds, allowing the reaction to proceed more quickly.
Active Site
- The active site is the region of an enzyme where substrate binding and catalysis occur.
- The active site is typically a cleft or pocket on the enzyme surface that is lined with amino acid residues that participate in substrate binding and catalysis.
Systems Multienzyme
- Systems multienzyme are complexes of multiple enzymes that work together to catalyze a series of reactions.
- Examples of systems multienzyme include fatty acid synthase and pyruvate dehydrogenase complex.
Regulation of Enzyme Activity
- Enzyme activity can be regulated through various mechanisms, including substrate inhibition, allosteric regulation, and covalent modification.
Inhibition of Enzyme Activity
- Enzyme inhibitors can be classified into competitive, non-competitive, and uncompetitive inhibitors.
- Competitive inhibitors bind to the active site, preventing substrate binding, while non-competitive inhibitors bind to an allosteric site, changing the enzyme's conformation and reducing activity.
Industrial Applications of Enzymes
- Enzymes are used in various industries, including food, detergent, and pharmaceutical industries.
- Examples of enzymes used in industry include papain, amylase, and lipase.
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Description
Quiz about enzymes in nutrition, covering their role as catalysts, classification, and graphical representation of enzyme-catalyzed reactions.