55 Questions
What is the definition of an allosteric site?
Location on an enzyme that allows substances to bind in order to activate or inhibit enzymatic activity
What is the main difference between the Lock and Key model and the Induced Fit model of enzyme-substrate binding?
Lock and Key model requires an exact fit, while Induced Fit model allows for slight conformational changes in both enzyme and substrate
In noncompetitive regulation, where do the regulating molecules bind?
Allosteric site of an enzyme
What happens in competitive inhibition?
Other substances directly bind to the active site, blocking the desired substrate from binding
What is the defining characteristic of saturated fatty acids?
They contain no double bonds
What is the primary function of triacylglycerols in the body?
Store lipids in our bodies
What is the role of cholesteryl esters in the body?
Form a large group of plaque in the arteries
What is the function of bile salts in the body?
Solubilize dietary lipids in the small intestines
What is the primary function of steroid hormones?
Critical for sexual development, reproduction, and regulation of mineral balance
When are ketone bodies made in the body?
In times of energetic scarcity
What is the primary function of glycoproteins in the body?
Proteins with some amount of carbohydrate modification
What is the function of glycolipids in the body?
Membrane phospholipids with a carbohydrate moiety
What is the role of proteoglycans in the body?
Polysaccharide mesh nets joined to fibrous proteins
What is the primary function of peptidoglycans in the body?
Long polysaccharide chains cross-linked by peptides
What is the essential role of cholesterol in the body?
Essential for synthesis of important molecules and maintains membrane fluidity
What is the function of cholesteryl esters in the body?
Form a large group of plaque in the arteries
What does the Michaelis-Menten constant (Km) represent in enzyme kinetics?
The substrate concentration at which the reaction rate is half of Vmax
Which type of inhibitor binds to the enzyme at a site other than the active site and does not compete with the substrate?
Non-competitive inhibitor
What is the primary function of glycolysis in cellular metabolism?
To convert glucose into pyruvate under aerobic conditions
What is the main function of polysaccharides in cells?
Serve as energy storage and structural components
What is the process of synthesizing glucose from pyruvate, lactate, glycerol, and amino acids called?
Gluconeogenesis
What is the primary function of lipid molecules in cells?
Serve as energy storage, structural components, and signaling molecules
What is the primary function of ketone body metabolism in the body?
To produce and utilize ketone bodies during fasting or low-carbohydrate diets
What type of regulation can inhibit or activate enzymes by binding to allosteric sites?
Allosteric regulation
What type of enzyme catalysis involves the direct involvement of amino acid side chains in the catalytic mechanism?
General acid-base catalysis
What is the process of converting pyruvate into acetyl-CoA under aerobic conditions called?
Pyruvate oxidation
What type of inhibitor binds to the enzyme-substrate complex, preventing the release of product?
Uncompetitive inhibitor
What is the primary function of an allosteric site on an enzyme?
To allow substances to bind in order to activate or inhibit enzymatic activity
In the Lock and Key model of enzyme-substrate binding, what is the requirement for catalyzation to occur?
The substrate must be an exact fit for the enzyme's conformation
What happens in noncompetitive regulation of enzyme activity?
Molecules bind to the allosteric site of an enzyme to change its conformation
What is the effect of competitive inhibition on enzymatic activity?
The active site is blocked and the desired substrate cannot bind, inhibiting catalytic activity
What is the defining characteristic of the Induced Fit model of enzyme-substrate binding?
The enzyme binds the substrate loosely, then undergoes conformational change for a perfect fit
What is the function of competitive inhibition in enzyme regulation?
To block the active site and inhibit enzymatic activity
What is the main function of proteases in the body?
Catalyzing the degradation of proteins
What is the primary function of zymogens in covalent modification of proteins?
Activating enzymes
What is the net yield of ATP molecules in glycolysis from the metabolism of one glucose molecule?
2
What is the process of converting pyruvate into acetyl-CoA under aerobic conditions called?
Pyruvate oxidation
What is the primary function of ketone body metabolism in the body?
Providing alternative fuel during fasting or low-carbohydrate diets
What is the defining characteristic of steroid metabolism?
Involvement in the synthesis and degradation of steroid hormones, bile acids, and cholesterol
What is the defining characteristic of glycolipids in the body?
They are membrane phospholipids with a carbohydrate moiety
What is the primary function of sphingolipids in the body?
Form membranes
What is the main function of cholesteryl esters in the body?
Store lipids in our bodies
What is the primary function of bile salts in the body?
Solubilize dietary lipids in the small intestines
What is the primary function of proteoglycans in the body?
Contribute to the structural integrity of extracellular matrix and cell signaling
What is the defining characteristic of steroid hormones?
They are critical for sexual development, reproduction, and regulation of mineral balance in higher organisms
What is the primary function of ketone bodies in the body?
Provide energy to tissues such as the brain when glucose is not available
What is the main function of glycoproteins in the body?
Anchor proteins to the outer plasma membrane leaflet
Which type of lipid is amphiphilic and serves to insulate organs?
Triacylglycerols
What is the defining characteristic of unsaturated fatty acids?
Cis configuration
What is the primary function of cholesteryl esters in the body?
Storing lipids
What is the main role of bile salts in the body?
Solubilizing dietary lipids
What is the essential role of cholesterol in the body?
Maintaining membrane fluidity
What is the primary function of steroid hormones?
Critical for sexual development
What is the main function of glycolipids in the body?
Membrane phospholipids with a carbohydrate moiety
What is the role of proteoglycans in the body?
Polysaccharide mesh nets joined to fibrous proteins
Study Notes
Enzyme Kinetics and Regulation, Carbohydrates, Glycolysis, Gluconeogenesis, Lipids and Membranes Overview
- Enzymes catalyze reactions involving gaining or losing electrons, breaking double bonds, transferring groups, rearranging molecules, cleaving bonds with water, and joining molecules
- Enzymes increase reaction rates by increasing stability of intermediates and lowering activation energy
- Central equations for enzyme kinetics include Vo (Initial Velocity), Vmax (maximum catalytic velocity), [S] (Substrate Concentration), and Km (Michaelis Constant)
- When enzymes are saturated with substrate, the reaction rate becomes steady and tends towards Vmax
- Competitive, non-competitive, and mixed inhibitors can regulate enzyme activity
- Types of enzyme catalysts include general acid-base catalysts, metal ion catalysis, covalent catalysis, and amino acid side chains
- Proteases are enzymes that degrade proteins, such as serine protease (Chymotrypsin)
- Enzyme regulation can occur through altering gene expression, isolating enzymes in specific parts of the cell or body, and limiting enzyme-substrate interaction
- Covalent modification of proteins includes proteolytic cleavage, zymogens, and phosphorylation
- Allosteric regulation can inhibit or activate enzymes by binding to allosteric sites
- Monosaccharides are classified by the number of carbons and can undergo modifications such as amino sugars, acylation, and reduction to sugar alcohols
- Polysaccharides serve as energy storage (e.g., glycogen, amylose) and structural components (e.g., cellulose, chitin) in cells. Glycolysis is a ten-step anaerobic process that converts glucose into pyruvate, yielding two net ATP and two net NADH/H⁺ molecules. Gluconeogenesis is the synthesis of glucose from pyruvate, lactate, glycerol, and amino acids, and its control is reciprocal with glycolysis. Pyruvate can be converted into acetyl-CoA under aerobic conditions and into lactate or ethanol under anaerobic conditions. Lipid molecules are unique due to their hydrophobic nature, serving as energy storage, structural components, and signaling molecules. Ketone body metabolism involves the production and utilization of ketone bodies during fasting or low-carbohydrate diets. Steroid metabolism includes the synthesis and degradation of steroid hormones, bile acids, and cholesterol.
Enzyme Kinetics and Regulation, Carbohydrates, Glycolysis, Gluconeogenesis, Lipids and Membranes Overview
- Enzymes catalyze reactions involving gaining or losing electrons, breaking double bonds, transferring groups, rearranging molecules, cleaving bonds with water, and joining molecules
- Enzymes increase reaction rates by increasing stability of intermediates and lowering activation energy
- Central equations for enzyme kinetics include Vo (Initial Velocity), Vmax (maximum catalytic velocity), [S] (Substrate Concentration), and Km (Michaelis Constant)
- When enzymes are saturated with substrate, the reaction rate becomes steady and tends towards Vmax
- Competitive, non-competitive, and mixed inhibitors can regulate enzyme activity
- Types of enzyme catalysts include general acid-base catalysts, metal ion catalysis, covalent catalysis, and amino acid side chains
- Proteases are enzymes that degrade proteins, such as serine protease (Chymotrypsin)
- Enzyme regulation can occur through altering gene expression, isolating enzymes in specific parts of the cell or body, and limiting enzyme-substrate interaction
- Covalent modification of proteins includes proteolytic cleavage, zymogens, and phosphorylation
- Allosteric regulation can inhibit or activate enzymes by binding to allosteric sites
- Monosaccharides are classified by the number of carbons and can undergo modifications such as amino sugars, acylation, and reduction to sugar alcohols
- Polysaccharides serve as energy storage (e.g., glycogen, amylose) and structural components (e.g., cellulose, chitin) in cells. Glycolysis is a ten-step anaerobic process that converts glucose into pyruvate, yielding two net ATP and two net NADH/H⁺ molecules. Gluconeogenesis is the synthesis of glucose from pyruvate, lactate, glycerol, and amino acids, and its control is reciprocal with glycolysis. Pyruvate can be converted into acetyl-CoA under aerobic conditions and into lactate or ethanol under anaerobic conditions. Lipid molecules are unique due to their hydrophobic nature, serving as energy storage, structural components, and signaling molecules. Ketone body metabolism involves the production and utilization of ketone bodies during fasting or low-carbohydrate diets. Steroid metabolism includes the synthesis and degradation of steroid hormones, bile acids, and cholesterol.
Test your knowledge of enzyme kinetics, carbohydrate metabolism, glycolysis, gluconeogenesis, lipid structure, and membrane function with this comprehensive overview quiz. From enzyme regulation to monosaccharide modifications and metabolic pathways, this quiz covers key concepts in biochemistry.
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