Biochemistry Final Exam Flashcards
Humans are which of the following:
A) photoautotrophs
B) chemoautotrophs
C) photoheterotrophs
D) chemoheterotrophs
D) chemoheterotrophs
Cyanobacteria are:
A) photoautotrophs
B) chemoautotrophs
C) photoheterotrophs
D) chemoheterotrophs
A) photoautotrophs
You discover a new single-celled organism in a salt lake. Subsequent laboratory experiments reveal that the organism can live in the presence or absence of oxygen. This organism would most likely be classified as a:
A) an obligate anaerobe in the Bacterial domain.
B) an obligate anaerobe in the Archaeal domain.
C) a facultative anaerobe in the Archaeal domain.
D) a facultative anaerobe in the Bacterial domain.
C) a facultative anaerobe in the Archaeal domain.
Which organelle is found in both plant and animal cells?
A) starch granule
B) chloroplast
C) mitochondria
D) glyoxysome
C) mitochondria
Differential centrifugation is based on the differences in sedimentation rate of biological particles of different ______.
A) density
B) size and density
C) size
D) structure
B) size and density
Supramolecular complexes, such as chromatin, are held together by:
A) covalent bonds between monomeric units.
B) noncovalent interactions, such as hydrogen bonds.
C) covalent bonds between macromolecules.
D) interactions between the cytoskeleton and organelles.
B) noncovalent interactions, such as hydrogen bonds.
Important functional groups in biomolecules include:
A) lipids
B) thioesters
C) nucleic acids
D) carbons
B) thioesters
Proteins are classified as macromolecules because they:
A) can associate noncovalently into very large structures.
B) are polymers with molecular weights above ~5,000 Da.
C) can function as enzymes, structural elements, signal receptors, or transporters.
D) are composed of multiple oligomers.
B) are polymers with molecular weights above ~5,000 Da.
What nucleobase is not present in DNA?
A) cytosine
B) adenine
C) guanine
D) uracil
D) uracil
A living organism is a(n):
A) isolated system
B) closed system
C) open system
D) universe
C) open system
Molecules that differ in configuration cannot be:
A) stereoisomers
B) cis-trans isomers
C) chiral centers that are mirror images of each other
D) chiral centers that can be interchanged by rotation of a single bond.
D) chiral centers that can be interchanged by rotation of a single bond.
Enantiomers:
A) are only associated with amino acids.
B) can be specific types of diastereomers.
C) are always designated either D or L.
D) can exist for molecules with more than one chiral carbon.
D) can exist for molecules with more than one chiral carbon.
An unusual characteristic of H20 is:
A) greater density in solid form (ice) than in liquid form (water).
B) high heat of vaporization.
C) low specific heat.
D) not readily forming intermolecular interactions.
B) high heat of vaporization.
Which atom does NOT commonly form hydrogen bonds between or within biological molecules?
A) oxygen
B) hydrogen
C) carbon
D) nitrogen
C) carbon
Which statement about hydrogen bonds is false?
A) They only occur between water molecules.
B) They are weak compared with covalent bonds.
C) They cause acid-base reactions in aqueous solutions to be very rapid.
D) They have optimal geometry.
A) They only occur between water molecules.
Dissolving table sugar into iced tea is an energetically favorable reaction due to a(n):
A) increase in enthalpy as heat moves into the sugar.
B) decrease in free energy due to broken weak interactions between sugar molecules.
C) increase in entropy as the sugar dissolves.
D) increase in free energy because there is no longer a solvation layer around the sugar crystal.
C) increase in entropy as the sugar dissolves.
Nonpolar compounds:
A) force surrounding H2O molecules to become ordered.
B) increase entropy when dissolved in water.
C) decrease enthalpy when dissolved in water.
D) interfere with the hydrogen bonds among H2O molecules.
D) interfere with the hydrogen bonds among H2O molecules.
I need to calculate the osmotic pressure of a solvent. I know the concentration of the solute and the temperature of the solution. What else do I need?
A) whether the solute dissociates into 2+ ion species.
B) the vapor pressure of the solvent.
C) the boiling point of the solvent.
D) whether the solute is hydrophobic or hydrophilic.
A) whether the solute dissociates into 2+ ion species.
Which condition would cause red blood cells to burst due to excess water passing through the plasma membrane?
A) placing the cells in a solution of higher osmolarity than is present within the cells.
B) placing the cells in a solution of amphipathic molecules.
C) adding a charged solute, such as NaCl, to the cell suspension.
D) placing the cells in a hypotonic solution.
D) placing the cells in a hypotonic solution.
The pH of an aqueous solution:
A) must remain at 7.
B) is not affected by added OH-.
C) depends solely on the ionization of water.
D) is a function of the hydrogen ion concentration (to a reasonable approximation).
D) is a function of the hydrogen ion concentration (to a reasonable approximation).
When H2O ionizes:
A) the △G° = 0 kJ/mol.
B) it has a measurable Keq.
C) its concentration (7 M) does not appreciably change.
D) free H+ ions are present in solution.
B) it has a measurable Keq.
Weak acids:
A) only partially ionize in water.
B) have a pKa < 7.
C) react very slowly with bases.
D) are formed by dilution of strong acids.
A) only partially ionize in water.
The pKa of a weak acid:
A) is a function of its concentration.
B) is the pH at which it has no net charge.
C) is <0 at pH >7.
D) can be determined from its titration curve.
D) can be determined from its titration curve.
What is the actual function of a buffer system such as acetate/acetic acid?
A) to maintain a constant pH in the event that the concentration of an acid or base increases.
B) to maintain the solution at the pKa.
C) to ensure the solution has no free H+ or OH- within a specific range.
D) to keep the solution within one pH unit of the pKa.
A) to maintain a constant pH in the event that the concentration of an acid or base increases.
I need to calculate the pH of a weak acid. I know the concentration of the acid and its conjugate base, and my solution is at 30° C. Using the Henderson-Hasselbach equation, what else do I need?
A) the Kd for H+ of the acid.
B) the total H+ concentration (that is, free and bound to the acid)
C) the free-energy change for the release of the H+.
D) the pKa of the acid.
D) the pKa of the acid.
Which statement about buffers is false?
A) they have a maximum buffering capacity at pH 7.
B) they are weak acids and bases.
C) [A-] = [HA] when pH = pKa.
D) they can sometimes be biological macromolecules.
A) they have a maximum buffering capacity at pH 7.
Which amino acid(s) has three pKa values?
A) leucine
B) proline
C) lysine
D) threonine
E) cysteine
C) lysine
E) cysteine
Which amino acid would most likely be found in the interior of a globular protein?
A) Val
B) D
C) Aspartate
D) Cysteine
E) Y
A) Val
Given that all 20 common amino acids have at least two oppositely charges groups, which statement is NOT correct?
A) solutions of amino acids can act as buffers.
B) all amino acids are zwitterions.
C) all amino acids carry at least one charge across the full range of their titration curves.
D) amino acid isoelectric points should be near neutrality.
E) it is not possible to fully deprotonate amino acids.
E) it is not possible to fully deprotonate amino acids.
At what pH values will histidine have a net neutral charge?
A) below 1.82
B) between 1.82 and 6.0
C) between 6.0 and 9.17
D) above 9.17
E) there are no pH values where histidine will have a net neutral charge.
C) between 6.0 and 9.17
Which statement is correct about peptides?
A) Peptides have no alpha-carboxyl groups.
B) Peptides have their amino acid sequences written from the N-terminus.
C) Peptides do not have isoelectric points.
D) Peptides are not biologically active.
E) Peptide bonds are broken through condensation reactions.
B) Peptides have their amino acid sequences written from the N-terminus.
Which statement is correct about proteins?
A) Proteins can consist of more than one polypeptide chain.
B) Proteins consist solely of polymerized amino acids.
C) Proteins all have similar amino acid compositions.
D) Proteins can, by definition, consist of no more than 2,000 amino acid residues.
E) Proteins do not have ionizable groups.
A) Proteins can consist of more than one polypeptide chain.
Which protein would elute first from a gel filtration column?
A) Protein A, with Mr=27,000
B) Protein B, with Mr=58,000
C) Protein C, a homodimer with promoter Mr=11,300
D) Protein D, with Mr=15,000
Mr: relative molecular weight
B) Protein B, with Mr=58,000
A new protein resembling myosin was reported. Unlike myosin, it binds calcium. Its isoelectric point and molecular weight are very similar to those of myosin. Which method would best separate the new protein from myosin if those two proteins were in the same buffer solution?
A) Ion-Exchange Chromatography
B) Size-Exclusion Chromatography
C) Affinity Chromatography
D) Dialysis
E) Fractionation
C) Affinity Chromatography
What measurement increases during purification of an enzyme?
A) Activity
B) Total Protein
C) Specific Activity
D) Fraction Volume
C) Specific Activity
Trypsin catalyzes the hydrolysis of peptide bonds in which a Lys or Arg residue contributes a carbonyl group LL-37, an antimicrobacterial peptide with 37 residues has 6 Lys residues and 5 Arg residues. How many smaller peptides will LL-37 yield upon trypsin cleavage?
A) 6
B) 5
C) 12
D) 37
E) 11
C) 12
Chemical synthesis of peptides by the Merrifield method:
A) involves synthesizing the peptide and then attaching it to a solid support.
B) is nearly as efficient as peptide bond synthesis in biochemical systems.
C) has a practical upper limit of a polymer of ~500 amino acid residues.
D) proceeds from the carboxyl terminus to the amino terminus.
D) proceeds from the carboxyl terminus to the amino terminus.
The heme prosthetic group:
A) consists of protoporphyrin and an iron (II) ion.
B) is found only in myoglobin and hemoglobin.
C) contains a single iron atom in its ferrous (Fe2+) state that has a total of 4 coordination bonds.
D) is only found bound to protein.
A) consists of protoporphyrin and an iron (II) ion.
Myoglobin:
A) has a quaternary structure.
B) contains a pocket for binding heme that is made up of largely the C and D helices.
C) contains multiple binding sites for O2.
D) consists mostly of alpha-helices.
D) consists mostly of alpha-helices.
Protein A has a binding site for ligand L with a Ka of 10^8 M^-1. Protein B has a binding site for ligand L with a Ka of 10^5 M^-1. Which protein has the higher affinity for ligand L?
A) Protein A
B) Protein B
C) It is not possible to determine based on only Ka values.
A) Protein A
Protein A has a Ka = 6.0 µM^-1 for binding ligand L. Protein B has a Kd=4.0 µM for binding ligand L. Based on this information, which statement is true?
A) Protein B binds L with higher affinity.
B) Protein A is half-saturated with L when [L] is 6.0 µM^-1.
C) The Ka of protein B for L is 0.25 µM^-1.
D) When [L] =1 µM, Y=0.17 for protein A.
C) The Ka of protein B for L is 0.25 µM^-1.
When the partial pressure of oxygen is equal to the P50 of myoglobin, what is the value of Y?
A) 0.0
B) 0.25
C) 0.50
D) 0.75
E) 1.00
C) 0.50
Oxygen carried by whole blood in animals is bound and transported by hemoglobin in what type of cell?
A) Hemoblastcytes
B) Erythrocytes
C) White Blood Cells
D) Stem Cells
E) Neurons
B) Erythrocytes
The alpha and beta subunits of hemoglobin:
A) each contain 4 heme prosthetic groups.
B) contain several stretches of identical amino acids.
C) are both tetramers.
D) have high structural similarity to each other.
E) differ in sequence and structure.
D) have high structural similarity to each other.
The T→R transition is triggered by:
A) ion pairs forming between residues and O2 at the A1B2 (and A2B1) interface.
B) the structures of the individual subunits changing.
C) O2 causing the heme to assume a more planar conformation, shifting the position of the His F8 and the F helix.
D) AB subunit pairs sliding past each other and rotating, narrowing the pocket between the alpha subunits.
C) O2 causing the heme to assume a more planar conformation, shifting the position of the His F8 and the F helix.
Leghemoglobin is an oxygen-binding protein in root nodules that contain bacteria and fix atmospheric nitrogen. Which statement is true is leg hemoglobin is like myoglobin and not hemoglobin?
A) There are four oxygen-binding sites.
B) The oxygen-binding curve is hyperbolic.
C) There is cooperative oxygen binding.
D) The oxygen-binding curve is sigmoidal.
E) Oxygen binding changes the heme configuration from T to R.
B) The oxygen-binding curve is hyperbolic.
Which molecule is a homotropic modulator of oxygen binding to hemoglobin?
A) Oxygen
B) H+
C) Carbon Dioxide
D) Hemoglobin
E) Carbon Monoxide
A) Oxygen
A newly discovered protein has multiple subunits, each with a single ligand-binding site. Binding of the ligand to one site increases the binding affinity of other sides for the ligand. The Hill coefficient (nH) is:
A) Equal to 1
B) Greater than 1
C) Less than 1
D) Not able to be calculated.
B) Greater than 1
There are 2 binding sites for acetylcholine (neurotransmitter) on its receptor. What would be the shape of a Hill plot if there were cooperatively of binding?
A) Hyperbolic
B) Linear
C) Sigmoidal, with a sharp change in slope.
D) Two sigmoidal areas linked together, one for each binding event.
E) Two sigmoidal lines, one higher than the other on the graph.
C) Sigmoidal, with a sharp change in slope.
In peripheral tissues:
A) The affinity of hemoglobin for oxygen increases and the protein binds more O2.
B) CO2 is excreted.
C) The structural effects of H+ and CO2 binding to hemoglobin favor the R state.
D) O2 is released.
D) O2 is released.
What is the actual, significant effect of 2,3-biphosphoglycerate on oxygen binding by hemoglobin?
A) There is an increase in Kd for oxygen in peripheral tissues.
B) A higher concentration of oxygen can bind at high altitudes compared to low altitudes.
C) The affinity of hemoglobin for oxygen in peripheral tissues increases at high altitudes.
D) Heme further decreases affinity for both CO2 and H+ in lungs, allowing more O2 to bind.
E) It has no effect on O2 affinity, but it forces heme into the R state.
A) There is an increase in Kd for oxygen in peripheral tissues.
Which statement is false?
A) Hemoglobin can be considered a dimer of alpha-beta dimers.
B) O2 binding to myoglobin is allosteric but not cooperative.
C) 2,3-biphosphoglycerate decreases the affinity of hemoglobin for O2.
D) Fetal hemoglobin has a lower affinity for BPG than normal adult hemoglobin.
E) The Glu6 to Val6 that causes sickle cell anemia produces a hydrophobic patch on hemoglobins surface.
B) O2 binding to myoglobin is allosteric but not cooperative.
The molecular structure for which individual antibody or T-cell receptor is specific is known as:
A) An epitope
B) It’s target
C) An immune response
D) An immunoglobulin fold
A) An epitope
Which statement is false?
A) T lymphocytes produce immunoglobulins.
B) Immunoglobulins target foreign bacteria and viruses for destruction.
C) Memory cells allow the body to quickly respond to viruses it has encountered before.
D) Clonal selection increases the number of immune system cells that can respond to a particular pathogen.
E) Vaccines stimulate the production of memory cells.
A) T lymphocytes produce immunoglobulins.
Which description is associated with immunoglobulin G?
A) Consists of two Fc fragments and two Fab fragments.
B) Consists of one heavy and one light chain.
C) Most abundant immunoglobulin.
D) Important in the allergic response.
C) Most abundant immunoglobulin.
Which biochemical principle is not true of immunoglobulins as examples of protein structure and function?
A) Disulfide linkages strengthen the quaternary structure.
B) Because the antigen-binding domain has high affinity, there is no observed induced fit.
C) Amino acid chain flexibility and bond rotation permit optimal epitope binding.
D) There are two specific and identical binding sites with high affinity on the same molecule.
E) There is 100% sequence homology between the two antigen-binding sites.
B) Because the antigen-binding domain has high affinity, there is no observed induced fit.
Polyclonal antibodies:
A) Are synthesized by a population of identical B cells.
B) All recognize the same epitope.
C) Are identical to monoclonal antibodies.
D) Are used as analytic reagents in Western blot assays.
D) Are used as analytic reagents in Western blot assays.
Which biochemical structure is NOT present in myosin?
A) A motif
B) A fibrous region
C) A globular region
D) A prosthetic group
E) An enzyme
D) A prosthetic group
Thin filaments:
A) Only consist of F actin.
B) Are the only type of filament in the A band.
C) Assemble as successive monomeric actin molecules add to one end.
D) Are rodlike structures.
C) Assemble as successive monomeric actin molecules add to one end.
Which of the major proteins involved in muscle contraction hydrolyzes ATP?
A) Actin
B) Troponin
C) Myosin
D) Tropomyosin
C) Myosin
Enzymes:
A) Are proteins (with few exceptions).
B) Can be denatured and still retain full activity.
C) Have names always ending in “-ase.”
D) Are also referred to as
“coenzymes.”
A) Are proteins (with few exceptions).
In enzymes, which inorganic ion does NOT serve as a cofactor?
A) Zn2+
B) Cu2+
C) Ca2+
D) Mg2+
C) Ca2+
An apoenzyme:
A) Is the nonprotein component of a holoenzyme.
B) Always requires an inorganic ion for its activity.
C) Requires a cofactor for its activity.
D) Is an enzyme consisting of RNA rather than protein.
C) Requires a cofactor for its activity.
Some enzymes require an inorganic ion for catalytic function. When this inorganic ion is very tightly or covalently bound by the enzyme it is called a(n):
A) Apoenzyme
B) Prosthetic Group
C) Holoenzyme
D) Catalyst
B) Prosthetic Group
______ is NOT an E.C. class name for enzymes.
A) Transferases
B) Polymerases
C) Lyases
D) Isomerases
B) Polymerases
What is the free-energy starting point for a reverse reaction designated as?
A) Transition State
B) Ground State
C) Biochemical Standard Free Energy
D) Activation Energy
B) Ground State
The conversion of sucrose to CO2 and water has a very large and negative △G’°. Why is the conversion NOT spontaneous?
A) Only some reactions have a negative △G’°.
B) Conversion requires heat and O2.
C) Conversion requires the presence of cofactors.
D) There is a very large activation barrier.
D) There is a very large activation barrier.
What does an enzyme change relative to an uncatalyzed reaction?
A) The equilibrium constant.
B) The rate of the reaction.
C) The pH.
D) The free energy change of the reaction.
B) The rate of the reaction.
Which statement is true regarding the relationship between the biochemical standard free-energy change and the equilibrium constant, Keq?
A) The relationship between free-energy change and equilibrium is exponential.
B) A decrease in Keq translates into a more negative free energy.
C) The higher the temperature, the less the reaction favors product formation.
D) Small changes in free energy can lead to large changes in equilibria.
D) Small changes in free energy can lead to large changes in equilibria.
If a first-order reaction for the unimolar reaction S →P has a rate constant k of 0.05s^-1, how is this interpreted qualitatively?
A) 0.05% of the available S will be converted to P in 1 second.
B) 5% of the available S will be converted to P in 1 second.
C) 0.05% of the available P will be converted to S in 1 second.
D) 5% of the available P will be converted to S in 1 second.
B) 5% of the available S will be converted to P in 1 second.
How does the concept of “induced fit” support the current theory of substrate-enzyme interaction?
A) Enzyme structure is rigid, allowing for competition for the active site and easy ejection of the final product.
B) Enzyme conformational changes demonstrate feedback regulation of the enzyme and the ability to “turn off” activity.
C) Having a rigid structure allows the enzyme to bind the substrate and stabilize the ES complex.
D) Enzyme conformation changes allow additional stabilizing interactions with the transition state and enhance the activity.
D) Enzyme conformation changes allow additional stabilizing interactions with the transition state and enhance the activity.
Binding energy is defined as the:
A) Energy derived from noncovalent enzyme-substrate interaction.
B) Energy derived from release of the product and release from the EP interaction.
C) Energy released from the conversion of ES to EP.
D) Difference in the uncatalyzed activation energy and catalyzed activation energy.
A) Energy derived from noncovalent enzyme-substrate interaction.
What is the primary source of the energy enzymes used to reduce activation energies?
A) Desolvation of the substrate
B) Kinetic energy from the transition state
C) Noncovalent enzyme-substrate interaction
D) Covalent enzyme-product interaction
C) Noncovalent enzyme-substrate interaction
How does the induced fit mechanism of enzyme catalysis work?
A) The enzyme assumes a conformation identical to the substrate.
B) The enzyme undergoes a conformational change to maximize weak interactions to the substrate.
C) The substrate binds to the active site of the enzyme.
D) The enzyme undergoes entropy reduction to accommodate substrate.
B) The enzyme undergoes a conformational change to maximize weak interactions to the substrate.
How does the concept of “induced-fit” support the current theory of substrate-enzyme interaction?
A) Enzyme structure is rigid, allowing for competition for the active site and easy ejection of the final product.
B) Enzyme conformational changes demonstrate feedback regulation of the enzyme and the ability to “turn-off” activity.
C) Having a rigid structure allows the enzyme to bind to the substrate and stabilize the ES complex.
D) Enzyme conformation changes allow additional stabilizing interactions with the transition state and enhance the activity.
D) Enzyme conformation changes allow additional stabilizing interactions with the transition state and enhance the activity.
Which statement about enzymes is false?
A) They lower the activation energy of a reaction.
B) They alter the overall thermodynamics of a reaction.
C) A substantial amount of their catalytic power results from binding of the substrate(s) through weak interactions.
D) They increase the rates of reactions by 10^5 fold to 10^17 fold.
B) They alter the overall thermodynamics of a reaction.
Which amino acid might be expected to have the least effect on the function of an enzyme if it replaces a Glu residue in the enzyme?
A) Gly
B) Lys
C) His
D) Asp
D) Asp
After you mix a substrate and an enzyme together, there is an initial transient period, the pre-steady state. What happens during the pre-steady state?
A) [Et] decreases until it reaches a constant level.
B) [S] decreases until it reaches a constant level.
C) [P] increases until it reaches a constant level.
D) [ES] increases until it reaches a constant level.
D) [ES] increases until it reaches a constant level.
Which statement is false about the saturation effect?
A) The maximum initial rate of the catalyzed reaction is observed.
B) Virtually all of the enzyme is present as the ES complex.
C) It is responsible for the linear increase of V0 with an increase in [S].
D) Further increases in [S] have no effect on rate.
C) It is responsible for the linear increase of V0 with an increase in [S].
For a specific substrate/enzyme system, which condition will ALWAYS result in an increase in V0 (assuming nothing else changes)?
A) A decrease in Km and an increase in Vmax.
B) An increase in pH.
C) An increase in [S].
D) A decrease in [Et].
A) A decrease in Km and an increase in Vmax.
In deriving the Michaelis-Menten equation, what is the steady-state assumption?
A) [P] is negligible and k2 can be ignored.
B) The rate of formation of ES is equal to the rate of its breakdown.
C) The amount of substate bound by the enzyme at any given time is negligible compared with the total [S].
D) The reaction is a one-substrate enzyme-catalyzed reaction.
B) The rate of formation of ES is equal to the rate of its breakdown.
What is the definition of Km, the Michaelis constant?
A) The rate at which enzyme is turning substrate into product at 1/2Vmax.
B) The V0 at 1/2 maximal [S].
C) The number of molecules of substrate converted to product per second.
D) The concentration of substrate at which the enzyme is operating at half its maximal velocity.
D) The concentration of substrate at which the enzyme is operating at half its maximal velocity.
The Km on a Lineweaver-Burk plot is:
A) Equal to the Y-intercept.
B) Equal to the slope of the line.
C) The reciprocal of the Y-intercept.
D) The negative reciprocal of the X-intercept.
D) The negative reciprocal of the X-intercept.
In drug design, a drug’s affinity for a selected target, such as an enzyme, is an important factor in assessing a drug’s potential. The higher the affinity, the better the candidate. Under conditions where Kd measures affinity, which drug would be the BEST candidate?
A) Drug A: 10^-4
B) Drug B: 10^-6
C) Drug C: 10^-8
D) Drug D: 10^-10
D) Drug D: 10^-10
The rate-limiting step of an enzyme-catalyzed reaction:
A) Is always the last step.
B) Has a rate constant equal to kcat.
C) Is always the fastest step.
D) Is always slower than the rate of diffusion of the substrate to the active site.
B) Has a rate constant equal to kcat.
Pepsin, a peptidase found in the stomach, it has an optimal pH of about 1.6. Normally the gastric juice pH is between 1 and 2. An individual experiencing heartburn dissolves baking soda in water and drinks the mixture to neutralize the stomach acid. What happens to pepsin activity in this case?
A) Activity will decrease due to a decrease in pH.
B) Activity will decrease due to an increase in pH.
C) Activity will increase due to a decrease in pH.
D) Activity will increase due to an increase in pH.
B) Activity will decrease due to an increase in pH.
Which statement is false for a competitive inhibitor?
A) It is often structurally similar to substrate.
B) It does not change Vmax.
C) It is irreversible.
C) It is irreversible.
Which statement is false for an uncompetitive inhibitor?
A) Uncompetitive inhibitors bind at a site distinct from the substrate active site.
B) Uncompetitive inhibitors bind only to the ES complex.
C) Uncompetitive inhibitors are reversible.
D) Uncompetitive inhibitors affect the apparent Km but not the Vmax.
D) Uncompetitive inhibitors affect the apparent Km but not the Vmax.
Which statement is true about both mixed inhibitors and uncompetitive inhibitors?
A) Both inhibitors bind to the active site of an enzyme.
B) Both inhibitors affect the Km but not the Vmax.
C) Both inhibitors can bind to the enzyme-substate complex.
D) Both inhibitors can bind to either the free enzyme or the enzyme-substrate complex.
C) Both inhibitors can bind to the enzyme-substate complex.
Which type of inhibitor binds to the active site of an enzyme and undergoes the initial steps of the reaction before combining irreversibly with the enzyme?
A) Mixed inhibitors.
B) Suicide inactivators.
C) Transition-state analogs.
D) Competitive inhibitors.
B) Suicide inactivators.