Podcast
Questions and Answers
What is the function of ligases?
What is the function of ligases?
- Paste two pieces together (make a chemical bond), uses ATP (correct)
- Rearrange the order of atoms in a molecule (isomerization)
- Break a chemical bond without using water
- Add water across a chemical bond (hydrolysis)
Which enzyme type is responsible for breaking a chemical bond by adding water across it?
Which enzyme type is responsible for breaking a chemical bond by adding water across it?
- Ligases
- Lyases
- Isomerases
- Hydrolases (correct)
Which coenzyme is a building block of Vitamin B1?
Which coenzyme is a building block of Vitamin B1?
- Thiamine Pyrophosphate (correct)
- Adenosine Monophosphate
- Lipoamide
- CoASH
What is the common theme associated with Coenzyme A?
What is the common theme associated with Coenzyme A?
Which enzyme type is responsible for rearranging the order of atoms in a molecule (isomerization)?
Which enzyme type is responsible for rearranging the order of atoms in a molecule (isomerization)?
What is the function of histidine (H57) in the active site of chymotrypsin?
What is the function of histidine (H57) in the active site of chymotrypsin?
Which class of proteases requires Ca++ as a cofactor and is found in Eukaryotes and Eubacteria, but not Archaea?
Which class of proteases requires Ca++ as a cofactor and is found in Eukaryotes and Eubacteria, but not Archaea?
Which enzyme is known for cleaving precursor proteins and is a homodimer with one active site per subunit?
Which enzyme is known for cleaving precursor proteins and is a homodimer with one active site per subunit?
Which protease has an active site composed of the amino acids His-His-Glu and requires Zn as a cofactor?
Which protease has an active site composed of the amino acids His-His-Glu and requires Zn as a cofactor?
In the liver, Alcohol Dehydrogenase (ADH) uses NAD+ to convert alcohols to which compound?
In the liver, Alcohol Dehydrogenase (ADH) uses NAD+ to convert alcohols to which compound?
Which term best describes the relationship between enzymes and effectors?
Which term best describes the relationship between enzymes and effectors?
In enzyme diversity, how many biological reactions/enzyme categories are typically recognized?
In enzyme diversity, how many biological reactions/enzyme categories are typically recognized?
Which enzyme is associated with the need for speed in enzyme catalysis?
Which enzyme is associated with the need for speed in enzyme catalysis?
What type of binding does hemoglobin demonstrate as a case study in enzyme diversity?
What type of binding does hemoglobin demonstrate as a case study in enzyme diversity?
In enzyme diversity, which term best describes the relationship between substrate binding and cooperativity?
In enzyme diversity, which term best describes the relationship between substrate binding and cooperativity?
How many families of carbonic anhydrases have been discovered?
How many families of carbonic anhydrases have been discovered?
What metal ion is used by the η family of carbonic anhydrases?
What metal ion is used by the η family of carbonic anhydrases?
What catalytic strategy is employed by the active site of carbonic anhydrases?
What catalytic strategy is employed by the active site of carbonic anhydrases?
What is the medical application of carbonic anhydrases related to artificial lungs?
What is the medical application of carbonic anhydrases related to artificial lungs?
How many splice variations of carbonic anhydrases are produced by humans?
How many splice variations of carbonic anhydrases are produced by humans?
What is the role of an apoenzyme?
What is the role of an apoenzyme?
In the context of enzyme diversity, which type of reaction results in swapping functional groups?
In the context of enzyme diversity, which type of reaction results in swapping functional groups?
What is the preferred state of ATCase when CTP binds to it?
What is the preferred state of ATCase when CTP binds to it?
What is the function of zymogens?
What is the function of zymogens?
What type of kinetics can multiple binding site enzymes follow if they are noncooperative?
What type of kinetics can multiple binding site enzymes follow if they are noncooperative?
What is the role of effector binding in enzyme function?
What is the role of effector binding in enzyme function?
What is the type of reaction catalyzed by serine proteases like chymotrypsin?
What is the type of reaction catalyzed by serine proteases like chymotrypsin?
What is the catalytic triad of chymotrypsin composed of?
What is the catalytic triad of chymotrypsin composed of?
What is the main catalytic strategy employed by carbonic anhydrases?
What is the main catalytic strategy employed by carbonic anhydrases?
Why do we need proteases like chymotrypsin?
Why do we need proteases like chymotrypsin?
What is the purpose of reversible covalent modifications in proteins?
What is the purpose of reversible covalent modifications in proteins?
Which type of molecule is Myristic Acid?
Which type of molecule is Myristic Acid?
What is the main contribution of carbohydrates to the proteome?
What is the main contribution of carbohydrates to the proteome?
Which color represents nucleotides in the structures referred to in the text?
Which color represents nucleotides in the structures referred to in the text?
What is the significance of ADP-ribose in reversible covalent modifications?
What is the significance of ADP-ribose in reversible covalent modifications?
What is the role of Farnesyl in reversible covalent modifications?
What is the role of Farnesyl in reversible covalent modifications?
What type of modification creates nonproteinogenic amino acids by adding functional groups to activate/inactivate enzymes?
What type of modification creates nonproteinogenic amino acids by adding functional groups to activate/inactivate enzymes?
What is the color used to represent fatty acids in the structures mentioned in the text?
What is the color used to represent fatty acids in the structures mentioned in the text?
In the context of enzyme diversity, what is the main difference between apoenzymes and holoenzymes?
In the context of enzyme diversity, what is the main difference between apoenzymes and holoenzymes?
When CTP binds to ATCase, what is the preferred state of the enzyme?
When CTP binds to ATCase, what is the preferred state of the enzyme?
What is the catalytic triad of chymotrypsin composed of?
What is the catalytic triad of chymotrypsin composed of?
What type of binding does hemoglobin demonstrate as a case study in enzyme diversity?
What type of binding does hemoglobin demonstrate as a case study in enzyme diversity?
What metal ion is used by the η family of carbonic anhydrases?
What metal ion is used by the η family of carbonic anhydrases?
What is the function of zymogens?
What is the function of zymogens?
What is the main contribution of carbohydrates to the proteome?
What is the main contribution of carbohydrates to the proteome?
What is the main catalytic strategy employed by carbonic anhydrases?
What is the main catalytic strategy employed by carbonic anhydrases?
What is the function of the oxyanion hole in chymotrypsin's active site?
What is the function of the oxyanion hole in chymotrypsin's active site?
Which class of proteases requires Ca++ as a cofactor and is found in Eukaryotes and Eubacteria, but not Archaea?
Which class of proteases requires Ca++ as a cofactor and is found in Eukaryotes and Eubacteria, but not Archaea?
What is the active site composition of the MMPs proteases?
What is the active site composition of the MMPs proteases?
Which metal ion is required by Thermolysin's active site for its function?
Which metal ion is required by Thermolysin's active site for its function?
What is the role of Renin in the body?
What is the role of Renin in the body?
Which active site residues are split over a heterodimer by Calpains?
Which active site residues are split over a heterodimer by Calpains?
What is the main role of Alcohol Dehydrogenase (ADH) in the liver?
What is the main role of Alcohol Dehydrogenase (ADH) in the liver?
8.106
8.106
What is the specific role of the S1 pocket in chymotrypsin's active site?
What is the specific role of the S1 pocket in chymotrypsin's active site?
What is the main role of HIV Protease in cleaving precursor proteins?
What is the main role of HIV Protease in cleaving precursor proteins?
What type of kinetics do Michaelis-Menten enzymes follow?
What type of kinetics do Michaelis-Menten enzymes follow?
In the context of reversible reactions, at equilibrium, what is the condition that must be satisfied?
In the context of reversible reactions, at equilibrium, what is the condition that must be satisfied?
What are the two important equilibrium constants defined for reversible reactions?
What are the two important equilibrium constants defined for reversible reactions?
What type of reaction does zero order kinetics represent?
What type of reaction does zero order kinetics represent?
What kinetics does a reversible reaction follow at equilibrium?
What kinetics does a reversible reaction follow at equilibrium?
What does the condition $k_1S = k_{-1}P$ signify in a reversible reaction?
What does the condition $k_1S = k_{-1}P$ signify in a reversible reaction?
In Michaelis-Menten kinetics, what is true about catalysis?
In Michaelis-Menten kinetics, what is true about catalysis?
What type of reaction is indicated by the condition $k_1S = k_{-1}P$ in a reversible reaction?
What type of reaction is indicated by the condition $k_1S = k_{-1}P$ in a reversible reaction?
Which type of kinetics do second-order reactions follow?
Which type of kinetics do second-order reactions follow?
What is true about catalysis according to Michaelis-Menten kinetics?
What is true about catalysis according to Michaelis-Menten kinetics?
In which type of kinetics do Michaelis-Menten enzymes follow?
In which type of kinetics do Michaelis-Menten enzymes follow?
What is the interpretation of the condition $k_1S = k_{-1}P$ in a reversible reaction?
What is the interpretation of the condition $k_1S = k_{-1}P$ in a reversible reaction?
Which type of reaction does zero order kinetics represent?
Which type of reaction does zero order kinetics represent?
What is the main difference between Michaelis-Menten enzymes and first order kinetics?
What is the main difference between Michaelis-Menten enzymes and first order kinetics?
What type of kinetics can multiple binding site enzymes follow if they are noncooperative?
What type of kinetics can multiple binding site enzymes follow if they are noncooperative?
In the context of Michaelis-Menten kinetics, what does the term 'Km' represent?
In the context of Michaelis-Menten kinetics, what does the term 'Km' represent?
What does the turnover number (kcat) in Michaelis-Menten kinetics indicate?
What does the turnover number (kcat) in Michaelis-Menten kinetics indicate?
What does the equilibrium constant (KS) in Michaelis-Menten kinetics define?
What does the equilibrium constant (KS) in Michaelis-Menten kinetics define?
How can the Michaelis-Menten model be simplified when not much product (P) is present and [E·P] is approximately 0?
How can the Michaelis-Menten model be simplified when not much product (P) is present and [E·P] is approximately 0?
What assumption allows the simplification of the Michaelis-Menten model to E + S ⇌ E·S → E + P?
What assumption allows the simplification of the Michaelis-Menten model to E + S ⇌ E·S → E + P?
What is the Michaelis-Menten equation in its most familiar form?
What is the Michaelis-Menten equation in its most familiar form?
What does it signify if k2 is the rate-limiting step in the Michaelis-Menten kinetics?
What does it signify if k2 is the rate-limiting step in the Michaelis-Menten kinetics?
What condition indicates that νmax is reached when the enzyme is fully saturated?
What condition indicates that νmax is reached when the enzyme is fully saturated?
What does the abbreviation $\nu_0$ represent in the context of Michaelis-Menten kinetics?
What does the abbreviation $\nu_0$ represent in the context of Michaelis-Menten kinetics?
What does the Michaelis constant ($K_m$) represent in Michaelis-Menten kinetics?
What does the Michaelis constant ($K_m$) represent in Michaelis-Menten kinetics?
What is the main difference between cooperative enzymes and noncooperative enzymes with respect to following Michaelis-Menten kinetics?
What is the main difference between cooperative enzymes and noncooperative enzymes with respect to following Michaelis-Menten kinetics?
In the context of enzyme kinetics, what does the condition $k_1S = k_{-1}P$ signify in a reversible reaction?
In the context of enzyme kinetics, what does the condition $k_1S = k_{-1}P$ signify in a reversible reaction?
Which catalytic strategy is commonly employed by enzymes according to Michaelis-Menten kinetics?
Which catalytic strategy is commonly employed by enzymes according to Michaelis-Menten kinetics?
What is the significance of the oxyanion hole in chymotrypsin's active site?
What is the significance of the oxyanion hole in chymotrypsin's active site?
What type of enzyme kinetics do cooperative enzymes exhibit?
What type of enzyme kinetics do cooperative enzymes exhibit?
In the context of Michaelis-Menten kinetics, what is the significance of the x-intercept in a Lineweaver-Burk plot?
In the context of Michaelis-Menten kinetics, what is the significance of the x-intercept in a Lineweaver-Burk plot?
How does the Hill coefficient (nH) differ in the context of cooperative binding as described by the Hill equation?
How does the Hill coefficient (nH) differ in the context of cooperative binding as described by the Hill equation?
What effect does a perfectly cooperative binder (n > 1) have on the approximation of θ in the Hill equation?
What effect does a perfectly cooperative binder (n > 1) have on the approximation of θ in the Hill equation?
What does a Hill plot of Hemoglobin with nH > 1 indicate about its binding characteristics?
What does a Hill plot of Hemoglobin with nH > 1 indicate about its binding characteristics?
How does the slope of a Hill plot relate to the level of cooperativity in ligand binding?
How does the slope of a Hill plot relate to the level of cooperativity in ligand binding?
What is the relationship described by the Hill equation?
What is the relationship described by the Hill equation?
In Michaelis-Menten kinetics, what does a poor enzyme with kcat > k-1 represent?
In Michaelis-Menten kinetics, what does a poor enzyme with kcat > k-1 represent?
What does the condition kcat/km = 1 indicate in the context of Michaelis-Menten kinetics?
What does the condition kcat/km = 1 indicate in the context of Michaelis-Menten kinetics?
What does the dissociation constant (KD) represent in terms of enzyme kinetics?
What does the dissociation constant (KD) represent in terms of enzyme kinetics?
What does the condition Km 𝜈0 = 𝜈max/2 indicate in Michaelis-Menten kinetics?
What does the condition Km 𝜈0 = 𝜈max/2 indicate in Michaelis-Menten kinetics?
What is the reaction rate for an IRREVERSIBLE reaction?
What is the reaction rate for an IRREVERSIBLE reaction?
Which representation of the reaction data is most suitable for determining the reaction order?
Which representation of the reaction data is most suitable for determining the reaction order?
What is the interpretation of the condition ν = k[S]n?
What is the interpretation of the condition ν = k[S]n?
What is the significance of the slope (k) in the linear response of 1/[S] vs. time?
What is the significance of the slope (k) in the linear response of 1/[S] vs. time?
What does the term 'hyperbolic' refer to in kinetics trends?
What does the term 'hyperbolic' refer to in kinetics trends?
In Michaelis-Menten kinetics, what does ν represent in the equation ν = νmax[S] / (Km + [S])?
In Michaelis-Menten kinetics, what does ν represent in the equation ν = νmax[S] / (Km + [S])?
What does the value of Km indicate in Michaelis-Menten kinetics?
What does the value of Km indicate in Michaelis-Menten kinetics?
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Study Notes
Enzyme Functions and Types
- Ligases are responsible for forming chemical bonds by condensing two molecules with the hydrolysis of ATP.
- Hydrolases break a chemical bond by adding water across it.
Coenzymes and Vitamins
- Thiamine (Vitamin B1) is a coenzyme that is a building block of Coenzyme A (CoA).
- Coenzyme A is associated with fatty acid metabolism and the common theme is energy production.
Enzyme Catalysis
- Isomerases are responsible for rearranging the order of atoms in a molecule (isomerization).
- Histidine (H57) is a key residue in the active site of chymotrypsin, a serine protease.
Proteases
- Calpains are a class of proteases that require Ca++ as a cofactor and are found in Eukaryotes and Eubacteria, but not Archaea.
- Chymotrypsin is a serine protease that cleaves precursor proteins and is a homodimer with one active site per subunit.
- Thermolysin is a metalloprotease that requires Zn as a cofactor.
Enzyme Diversity
- Enzyme diversity recognizes six biological reactions/enzyme categories.
- Carbonic anhydrases are associated with the need for speed in enzyme catalysis.
- Hemoglobin demonstrates cooperative binding, a case study in enzyme diversity.
Carbonic Anhydrases
- There are three families of carbonic anhydrases that have been discovered.
- The η family of carbonic anhydrases uses Zn as a cofactor.
- Carbonic anhydrases employ a catalytic strategy of metal-assisted acid-base catalysis.
- Carbonic anhydrases have a medical application related to artificial lungs.
- Humans produce 14 splice variations of carbonic anhydrases.
Enzyme-Substrate Binding
- Allosteric modulation occurs when an effector binds to an allosteric site, changing the enzyme's activity.
- In noncooperative enzymes, substrate binding does not affect the enzyme's activity.
- In cooperative enzymes, substrate binding affects the enzyme's activity, either positively or negatively.
Protease Functions
- Zymogens are inactive precursors of enzymes that are cleaved to form the active enzyme.
- Chymotrypsin is a serine protease that catalyzes peptide bond hydrolysis.
- The catalytic triad of chymotrypsin is composed of His-His-Glu.
- The oxyanion hole in chymotrypsin's active site stabilizes the negative charge on the tetrahedral intermediate.
Reversible Reactions and Kinetics
- Michaelis-Menten kinetics describe the kinetics of reversible reactions.
- In a reversible reaction, at equilibrium, the condition k1S = k-1P must be satisfied.
- The condition k1S = k-1P signifies that the reaction has reached equilibrium.
- Michaelis-Menten enzymes follow saturation kinetics.
- The turnover number (kcat) in Michaelis-Menten kinetics indicates the enzyme's maximum catalytic rate.
- The equilibrium constant (KS) in Michaelis-Menten kinetics defines the enzyme-substrate binding affinity.
- The Michaelis constant (Km) represents the enzyme's substrate binding affinity.
- Cooperative enzymes exhibit sigmoidal kinetics, while noncooperative enzymes follow Michaelis-Menten kinetics.
Hill Equation and Cooperative Binding
- The Hill equation describes cooperative binding in enzymes.
- The Hill coefficient (nH) represents the level of cooperativity in ligand binding.
- A Hill plot of Hemoglobin with nH > 1 indicates positive cooperativity in ligand binding.
Enzyme Inhibition and Regulation
- In reversible reactions, the dissociation constant (KD) represents the enzyme-inhibitor binding affinity.
- In Michaelis-Menten kinetics, a poor enzyme has kcat > k-1, indicating slow product release.
- The condition Km ν0 = νmax/2 indicates that the enzyme is operating at half-maximal velocity.
- The reaction rate for an irreversible reaction is given by the equation ν = k[S]^n.
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