Enzyme catalysis and vocabulary

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Questions and Answers

Which of the following is NOT a characteristic of enzyme catalysts?

  • They are highly specific.
  • They lower the activation energy of a reaction.
  • They increase the rate of a reaction.
  • They are consumed during the reaction. (correct)

How does a competitive inhibitor affect enzyme kinetics?

  • It decreases both the Vmax and the Km.
  • It decreases the Vmax but does not affect the Km.
  • It increases the Km but does not affect the Vmax. (correct)
  • It increases both the Vmax and the Km.

Which statement best describes the induced-fit model of enzyme-substrate interaction?

  • The active site of the enzyme adjusts its shape to better accommodate the substrate after initial binding. (correct)
  • The enzyme and substrate bind based on complementary charges only.
  • The substrate perfectly fits into the rigid active site of the enzyme.
  • The enzyme changes the substrate's shape to facilitate the reaction.

What is the primary role of protein kinases in cellular regulation?

<p>To add phosphate groups to proteins. (B)</p> Signup and view all the answers

Which of the following best describes the function of the enzyme catalase?

<p>It catalyzes the breakdown of hydrogen peroxide into water and oxygen. (B)</p> Signup and view all the answers

What is the significance of the Michaelis constant ($K_m$) in enzyme kinetics?

<p>It represents the substrate concentration at half the maximum velocity. (D)</p> Signup and view all the answers

How do allosteric enzymes differ from non-allosteric enzymes?

<p>Allosteric enzymes do not follow Michaelis-Menten kinetics. (D)</p> Signup and view all the answers

Which lipid type is the most abundant component of cell membranes?

<p>Phosphoglycerides (B)</p> Signup and view all the answers

What is the role of cholesterol in animal cell membranes?

<p>To increase membrane fluidity at low temperatures and decrease fluidity at high temperatures. (B)</p> Signup and view all the answers

Which transport mechanism requires energy input to move molecules against their concentration gradient?

<p>Active transport (D)</p> Signup and view all the answers

What are two molecules that can enter cells by diffusion in the absence of a transporter protein?

<p>oxygen and carbon dioxide</p> Signup and view all the answers

Flashcards

Catalyst

A substance that speeds up a chemical reaction without being consumed in the process.

Activation Energy (Ea)

The minimum energy required for a chemical reaction to occur.

Transition state

A temporary, high-energy intermediate state during a chemical reaction.

Active site

The specific region of an enzyme where substrate binding and catalysis occur.

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Induced-fit model

A model describing enzyme-substrate interaction where the enzyme changes shape upon substrate binding for an optimal fit.

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Initial reaction velocity (v)

The rate of a reaction at a specific point, usually measured at the beginning of the reaction.

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Michaelis Constant (Km)

The substrate concentration at which the reaction rate is half of Vmax.

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Maximum velocity (Vmax)

The maximum rate of an enzymatic reaction when the enzyme is saturated with substrate.

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Competitive inhibitor

A type of enzyme inhibition where the inhibitor binds to the active site, preventing the substrate from binding.

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Transport proteins

Membrane proteins that facilitate the movement of specific molecules across a biological membrane.

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Study Notes

Chapter 6 Vocabulary

  • Enzyme catalysis involves the acceleration of a reaction by a biological molecule.
  • Activation energy (Eᴀ) is the energy required to reach the transition state.
  • Transition state is an intermediate state during a reaction.
  • A metastable state is relatively stable but not at the lowest energy level.
  • A catalyst lowers the activation energy and increases reaction rate, but is not consumed. Enzymes are protein catalysts.
  • Ribozymes are RNA molecules with catalytic activity.
  • Active Site is the specific region of an enzyme where substrate binding and catalysis occur.
  • Prosthetic groups are non-amino acid components that contribute to protein structure and function.
  • Coenzymes are organic, non-protein molecules that assist enzymes in carrying out reactions.
  • Substrate specificity is the ability of an enzyme to bind to one specific substrate.
  • Hydrogenation is a chemical reaction involving the addition of hydrogen.
  • Group specificity is the ability of an enzyme to act on a range of substrates with a particular functional group.
  • The International Union of Biochemistry (IUB) Enzyme Commission (EC) developed a classification system of six major classes for enzymes.
  • Homeotherms are organisms that maintain a stable internal body temperature.
  • Denaturation is the process where proteins lose their structure, caused by heat, pH change or other factors.
  • The lock-and-key model is a simplified model on how enzymes and substrates fit.
  • The induced-fit model is a more accurate model that describes how the active site changes to bind to the substrate.
  • Substrate activation is when a substrate gains energy to reach the transition state.
  • There are three activation mechanisms like substrate binding, bond distortion and proton transfer.
  • Enzyme kinetics studies the rate of enzyme-catalyzed reactions.
  • Initial reaction velocity (v) is the rate of a reaction at the beginning, before much product has been formed.
  • Saturation is when all enzyme active sites are occupied.
  • Substrate concentration [S] is the molarity of the substrate.
  • Michaelis constant (Kᴍ) is the concentration of substrate at which the reaction rate is half of Vmax.
  • Maximum velocity (Vmax) is the highest possible rate of reaction when the enzyme is fully saturated with substrate.
  • Michaelis-Menten equation describes the rate of enzymatic reactions relating reaction rate to substrate concentration.
  • Turnover number (kcat) is the number of substrate molecules one enzyme molecule can convert per unit time.
  • The Lineweaver-Burk equation is a double reciprocal of the Michaelis-Menten equation, allowing Vmax and Km to be more easily determined.
  • Double-reciprocal plot helps visualize enzyme kinetics, and can be used to analyze different forms of inhibition.
  • Substrate analogs are compounds that resemble the substrate and bind to the active site, inhibiting the enzyme.
  • Allosteric effectors are molecules that bind to an enzyme somewhere, other than the active site, causing a change in its shape and affecting its activity.
  • Reversible inhibitors bind non-covalently and can dissociate, restoring enzyme activity.
  • Irreversible inhibitors bind covalently, permanently inactivating the enzyme.
  • Competitive inhibitors bind to the active site, preventing the substrate from binding.
  • Noncompetitive inhibitors bind to an allosteric site, changing the shape of the enzyme and reducing its activity.
  • Feedback inhibition is when the end product of a metabolic pathway inhibits an earlier enzyme in the pathway.
  • Substrate-level regulation is the direct control of enzyme activity by the levels of substrate and product.
  • Allosteric enzymes have multiple binding sites, and their activity is modulated by allosteric effectors.
  • Allosteric effectors bind to the other sites on the enzyme to change its activity.
  • An allosteric site is a location on an enzyme away from the active site that can bind molecules and modulate the enzyme's activity.
  • The active site is where the substrate binds and the chemical reaction occurs.
  • An allosteric inhibitor binds to the allosteric site to decrease the enzyme's activity.
  • An allosteric activator binds to the allosteric site to increase the enzyme's activity.
  • Catalytic subunits are the parts of a multi-subunit enzyme that contain the active sites and carry out the catalytic reaction.
  • Regulatory subunits bind regulatory molecules, or effectors, that modulate the catalytic activity of the enzyme.
  • Cooperativity is when the binding of one substrate molecule to an enzyme makes it easier for subsequent substrate molecules to bind.
  • Phosphorylation is the addition of a phosphate group to a molecule.
  • Covalent modification involves the formation or breaking of covalent bonds on an enzyme.
  • Protein kinase is an enzyme that adds phosphate groups to proteins.
  • Protein phosphatase is an enzyme that removes phosphate groups from proteins.
  • Dephosphorylation is the removal of a phosphate group from a molecule.
  • Phosphorylase is an enzyme that catalyzes the addition of phosphate groups to glycogen to break it down, and exists in two forms: a is active and b is inactive.
  • Phosphorylase kinase activates phosphorylase by phosphorylating it.
  • phosphorylase phosphatase inactivates phosphorylase a by removing a phosphate.
  • Glycogen synthase is an enzyme that catalyzes the conversion of glucose to glycogen.
  • Proteolytic cleavage is the activation of an enzyme from an inactive proenzyme.
  • Trypsinogen is an inactive precursor of trypsin, a digestive enzyme.
  • Trypsin is a digestive enzyme that breaks down proteins in the small intestine.
  • The pancreas is an organ that produces digestive enzymes and hormones.
  • Duodenum is the first section of the small intestine where digestion occurs.
  • Zymogen is an inactive enzyme precursor, requiring a biochemical change (such as hydrolysis) for it to become an active enzyme.
  • Hexapeptide is a peptide composed of six amino acids.
  • Enterokinase is an enzyme that converts trypsinogen into active trypsin.
  • Ribosomes are molecular machines that use RNA and proteins to synthesize proteins.
  • Ribozymes are RNA molecules that have catalytic activity.
  • Peptidyl transferase is an enzymatic activity of the ribosome responsible for forming peptide bonds during translation.

Chapter 7 vocabulary

  • The plasma membrane is a phospholipid bilayer that surrounds all cells, forming a selectively permeable barrier between the cell and its external environment.
  • Membrane transport refers to the movement of substances across the cell membrane, which includes passive and active transport.
  • Signal transduction is the process by which cells convert extracellular signals into intracellular responses.
  • Receptors are proteins on the cell surface or within the cell that bind specific molecules to initiate cellular responses.
  • The fluid mosaic model describes the structure of the plasma membrane as a dynamic arrangement of phospholipids and proteins.
  • Lipophilic substances are soluble in lipids or non-polar solvents.
  • Amphipathic molecules have both hydrophobic and hydrophilic regions.
  • Erythrocytes are red blood cells that facilitate oxygen transport in the blood.
  • A lipid bilayer is a thin polar membrane made of two layers of lipid molecules that form a continuous barrier around all cells.
  • The Davson-Danielli model is an outdated model describing the plasma membrane as a lipid bilayer sandwiched between two layers of proteins.
  • Polar pores are channels in the membrane that allow polar or charged molecules to pass through.
  • Trilaminar staining pattern is a staining pattern observed under electron microscopy, indicating a three-layered structure that was initially interpreted as support for the Davson-Danielli model.
  • Phospholipases are enzymes that hydrolyze phospholipids.
  • Peripheral proteins are located on the surface of the membrane and are easily removed without disrupting the membrane's structure.
  • Integral membrane proteins are permanently embedded within the lipid bilayer.
  • Transmembrane segments are the segments of an integral membrane protein that span the lipid bilayer.
  • Lipid-anchored proteins are located on the surface of the cell membrane that are covalently attached to lipid molecules embedded within the cell membrane.
  • Phospholipids are lipids containing a phosphate group.
  • Lipid rafts are cholesterol- and sphingolipid-enriched microdomains within the cell membrane.
  • Sterols are lipids with a characteristic four-ring structure.
  • Glycolipids consist of a carbohydrate attached to a lipid.
  • Sphingolipids are a class of lipids derived from sphingosine.
  • Phosphoglycerides are phospholipids with a glycerol backbone.
  • Phytosterols are plant-derived sterols similar to cholesterol which are important components of plant cell membranes.
  • Cholesterol is a key component of animal cell membranes that modulates their fluidity.
  • Transverse diffusion or flip-flop is the movement of a lipid molecule from one layer to the other.
  • Fatty acids are carboxylic acids with a long aliphatic tail.
  • Membrane asymmetry refers to the unequal distribution of lipids and proteins between the two leaflets of a cell membrane.
  • Rotation is the spinning or rotational movement of a lipid molecule within the plane of the membrane.
  • Lateral diffusion refers to the movement of lipid molecules and proteins within the plane of the cell membrane.
  • Flippases are enzymes that catalyze the movement of phospholipids from one leaflet to another.
  • Photobleaching is the photochemical destruction of a fluorophore, resulting in loss of fluorescence.
  • Fluorescence recovery is the return of fluorescence in a photobleached area due to the lateral movement of fluorescently labeled molecules.
  • Phase transition is the change in the state of a membrane from a fluid to a more solid or gel-like state due to decreased temperature.
  • Transition temperature (Tᴍ) is the specific temperature at which a membrane undergoes a phase transition.
  • Cis- vs. trans- fats involve distinct configurations of fatty acids around a double bond. Cis have substituents on the same side, creating a bend, while trans have substituents on opposite sides, resulting in a more linear structure.
  • Kinases are enzymes that phosphorylate molecules.
  • Freeze fracturing is a technique used to study membrane structure by splitting the lipid bilayer and examining the internal faces.
  • Integral membrane proteins are permanently embedded within the lipid bilayer.
  • Transmembrane proteins are integral membrane proteins that span the entire lipid bilayer.
  • Integral monotopic proteins are proteins that are bound to only one layer of the membrane.
  • Multipass proteins are transmembrane proteins that cross the lipid bilayer multiple times.
  • Singlepass proteins are transmembrane proteins that cross the lipid bilayer once.
  • β barrel is a type of protein structure that consists of beta strands forming a hollow cylindrical structure.
  • Multisubunit proteins are composed of multiple polypeptide chains.
  • Hydropathic analysis is used to identify hydrophobic and hydrophilic regions in a protein sequence, which can predict transmembrane domains.
  • Porins hydrophobicity plot is a plot that shows the hydrophobicity of amino acids along the protein sequence for porins.
  • DNA sequencing is the process of determining the precise order of nucleotides within a DNA molecule.
  • Liposomes are artificial vesicles made of lipid bilayers, used as models for cell membranes and drug delivery systems.
  • Site-directed mutagenesis is a technique used to create specific alterations in the DNA sequence of a gene.
  • Recombinant DNA is DNA that has been artificially combined from different sources.
  • Glycoprotein is a protein with carbohydrate molecules attached.
  • Epitope is the specific site on an antigen to which an antibody binds.
  • N-linked glycosylation is the attachment of a carbohydrate to the nitrogen atom of asparagine (Asn) residue in a protein.
  • Glycosylation is the process of adding carbohydrates to a molecule.
  • Glycocalyx is the carbohydrate coat on the outer surface of a cell.
  • O-linked glycosylation is the attachment of a carbohydrate to the oxygen atom of serine (Ser) or threonine (Thr) residue in a protein.
  • Fluorescent antibodies are antibodies labeled with a fluorescent dye, used to visualize and detect specific antigens in cells or tissues.
  • Cell fusion experiments are used to study membrane protein mobility and mixing by fusing two cells with different membrane markers.

Chapter 8 vocabulary

  • Selective permeability is a property of cellular membranes that allows only certain molecules to enter or exit the cell.
  • Secretion is the process by which cells release substances into the extracellular space.
  • Membrane transport encompasses the various mechanisms by which molecules cross cellular membranes.
  • Simple diffusion is the movement of molecules across a membrane down their concentration gradient without the aid of transport proteins.
  • Transport proteins are membrane-spanning proteins that facilitate the movement of specific molecules across a membrane.
  • Facilitated diffusion is the transport of molecules across a membrane down their concentration gradient with the aid of transport proteins.
  • Active transport is the movement of molecules across a membrane against their concentration gradient, requiring energy input.
  • A concentration gradient is the change in concentration of a substance from one area to another.
  • Channels are transmembrane proteins that form pores through which specific ions or molecules can pass.
  • The electrochemical potential is the driving force that determines the movement of ions across a membrane, considering both the concentration gradient and the electrical potential.
  • Osmosis is the movement of water across a semipermeable membrane from an area of high water concentration to an area of low water concentration.
  • Membrane potential (Vᴍ) is the difference in electrical potential between the interior and exterior of a cell.
  • Osmolarity is the concentration of a solution expressed as the total number of solute particles per liter.
  • A hypertonic solution has a higher solute concentration than another solution, causing cells to shrink as water moves out.
  • An isotonic solution has the same solute concentration as another solution, resulting in no net movement of water across cell membranes.
  • A hypotonic solution has a lower solute concentration than another solution, causing cells to swell as water moves in.
  • Counter-ions are ions that accompany the movement of charged molecules to maintain electrical neutrality.
  • Turgor pressure is the pressure exerted by the cell membrane against the cell wall in plant cells, resulting from the osmotic uptake of water.
  • Plasmolysis is the contraction of the protoplast of a plant cell as a result of loss of water from the cell.
  • A channel protein is a membrane protein that forms a hydrophilic pore through which specific molecules can pass.
  • A carrier protein is a membrane protein that binds to a specific molecule and undergoes a conformational change to transport it across the membrane.
  • The alternating conformation model suggests that carrier proteins undergo conformational changes to transport solutes across the membrane.
  • porins are channel-forming proteins found in the outer membrane of mitochondria and some bacteria, allowing the diffusion of small molecules.
  • A uniporter is a carrier protein that transports a single type of molecule across the membrane.
  • Coupled transport is the simultaneous transport of two or more molecules across a membrane, linked by a single carrier protein.
  • A symporter is a carrier protein that transports two different molecules across the membrane in the same direction.
  • An antiporter is a carrier protein that transports two different molecules across the membrane in opposite directions.
  • the anion exchange protein mediates the exchange of chloride and bicarbonate ions across the red blood cell membrane.
  • the glucose transporter (GLUT) is a membrane protein that facilitates the transport of glucose across the cell membrane.
  • Carbonic anhydrase is an enzyme that catalyzes the interconversion of carbon dioxide and water to bicarbonate and protons.
  • the chloride-bicarbonate exchanger is a membrane protein that facilitates the exchange of chloride and bicarbonate ions across the cell membrane.
  • Ion channels are membrane proteins that form pores allowing specific ions to pass through the membrane.
  • Transmembrane channels are channels that span the entire cell membrane.
  • β-barrel is a protein structure composed of beta strands that form a cylindrical channel through the membrane.
  • Directionality refers to the ability of a transport process to move molecules in a specific direction across the membrane.
  • Pumps (active transport) are transport proteins that use energy to move molecules against their concentration gradient.
  • Aquaporins (AQPs) are channel proteins that facilitate the rapid transport of water across the cell membrane.
  • Direct active transport uses ATP directly, while indirect active transport uses the movement of one molecule down its concentration gradient to power the movement of another.
  • Cystic Fibrosis (CF) is an inherited disorder caused by a mutation in the CFTR gene, leading to mucus buildup in various organs.
  • Lumen is the inside space of a tubular structure, such as the endoplasmic reticulum or the intestine.
  • CF Transmembrane Conductance Regulator (CFTR) is a protein a chloride channel protein responsible for regulating the transport of chloride ions across epithelial cell membranes.
  • ATPase pumps are enzymes that use the energy from ATP hydrolysis to transport ions or molecules across the membrane.
  • Multidrug resistance (MDR) transport protein is a membrane protein that pumps various drugs out of cells, leading to drug resistance in cancer cells and bacteria.
  • ATP synthase is an enzyme that synthesizes ATP from ADP and inorganic phosphate, using the proton gradient across the mitochondrial membrane.
  • Na+/K+ ATPase (pump) is an enzyme that uses ATP energy to pump sodium ions out of the cell and potassium ions into the cell, maintaining the electrochemical gradient.
  • Na+/glucose symporter is a membrane protein that transports both sodium ions and glucose across the membrane, using the sodium gradient as the driving force.
  • Bacteriorhodopsin is a light-driven proton pump found in archaea.

Chapter 9 vocabulary

  • Chemotrophs obtain energy by oxidizing chemical compounds.
  • Phototrophs obtain energy from sunlight.
  • Metabolism refers to the sum of all chemical reactions that occur within an organism.
  • Metabolic pathways are a series of interconnected chemical reactions.
  • Anabolic pathways are biosynthetic pathways that build complex molecules from simpler ones, requiring energy.
  • Catabolic pathways break down complex molecules into simpler ones, releasing energy.
  • Aerobic processes require the presence of oxygen.
  • Anaerobic processes occur in the absence of oxygen.
  • Energetic coupling is the process by which energy released from exergonic (energy-releasing) reactions is used to drive endergonic (energy-requiring) reactions.
  • Adenosine triphosphate (ATP) is the primary energy currency of the cell.
  • A phosphoester bond is a chemical bond that attaches a phosphate group to other molecules.
  • A phosphoanhydride bond is formed when two phosphate groups are linked together.
  • Adenosine is a nucleoside composed of adenine and ribose.
  • Adenosine diphosphate (ADP) is a nucleotide composed of a nitrogenous base. two phosphate groups, and a sugar.
  • Hydrolysis is the chemical breakdown of a compound due to reaction with water.
  • Adenosine monophosphate (AMP) is a nucleotide that contains on phosphate group, adenine, and ribose sugar.
  • Condensation is a chemical reaction in which two molecules combine to form a larger molecule, with the loss of a small molecule.
  • Charge repulsion refers to the repulsion between negatively charged phosphate groups in ATP, which contributes to its high energy content.
  • Resonance stabilization is the stabilization of a molecule due to the delocalization of electrons within its structure.
  • Resonance hybrid is a molecule that is best described as the average of two or more Lewis structures.
  • Oxidation is the loss of electrons from a molecule.
  • Group transfere reactions involve the transfer of a functional group.
  • Reduction is the gain of electrons by a molecule.
  • Chemotrophic energy metabolism is the process of obtaining energy from chemical compounds.
  • Dehydrogenation is the removal of hydrogen atoms from a molecule.
  • Hydrogenation is the addition of hydrogen atoms to a molecule.
  • Nicotinamide adenine dinucleotide (NAD+) is a coenzyme that functions as an electron carrier in redox reactions.
  • Niacin is a vitamin that is a precursor to NAD+.
  • The glucose aerobic respirat is the final electron acceptor in the electron transport chain.
  • Anaerobic respiration uses a different electron acceptor other than oxygen.
  • Fermentation is the metabolic process by which energy is extracted from glucose without oxygen.
  • Lactate fermentation is a type of anaerobic respiration that produces lactic acid
  • -alcohol fermentation is a type of anaerobic respiration that produces ethanol.
  • Glycolysis is the breakdown of glucose into pyruvate, producing a small amount of ATP and NADH.
  • Substrate-level phosphorylation is a metabolic reaction that results in the formation of ATP or GTP by the direct transfer of a phosphoryl group to ADP or GDP from another phosphrylated compound.
  • Phosphoolysis is the cleavage of a bond by the addition of a phosphate group.
  • Gluconeogenesis is the synthesis of glucose from non-carbohydrate precursors.
  • Bypass reactions are reactions that are used to circumvent irreversible steps in a metabolic pathway.
  • Sucrase is an enzyme that catalyzes the hydrolysis of sucrose into glucose and fructose.
  • Sucrose is a disaccharide consisting of glucose and fructose units.
  • Triacylglycerol is a fat molecule composed of three fatty acids attached to a glycerol backbone.

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