52 Questions
Which type of inhibitor binds to an enzyme at a location other than the active site?
Noncompetitive inhibitor
What is the primary effect of a competitive inhibitor on Vmax in enzyme kinetics?
Decrease Vmax
How does a noncompetitive inhibitor affect the Km value in enzyme kinetics?
No effect on Km
In terms of Lineweaver-Burk plot, how would a competitive inhibitor affect the slope of the line?
Increase the slope
Which type of inhibition involves a molecule that resembles the substrate and competes for the enzyme's active site?
Competitive inhibition
What is a characteristic feature of noncompetitive inhibitors regarding their interaction with enzymes?
They alter the enzyme's shape
What type of molecules are cofactors in enzyme kinetics?
Small non-protein molecules
Which of the following is NOT a cofactor mentioned in the text?
Acetyl CoA carboxylase
Where do zymogens play a role in enzyme kinetics?
Activating enzyme activity
What is the role of metal cofactors in enzyme kinetics?
Aid in enzyme activity
Which enzyme regulation mechanism involves noncompetitive inhibitors?
Allosteric regulation
In the Lineweaver-Burk plot, what effect does a competitive inhibitor have on the slope of the lines?
No effect on the slope
What type of inhibitors compete with the substrate for the active site of the enzyme?
Competitive inhibitors
How do noncompetitive inhibitors affect Vmax and Km?
Decrease Vmax, no effect on Km
What effect do competitive inhibitors have on a Lineweaver-Burk plot?
Lines intersect at a new point on the y-axis
Which type of inhibitor binds to an allosteric site on the enzyme rather than the active site?
Noncompetitive inhibitors
What is the effect of noncompetitive inhibitors on enzyme activity?
Decrease enzyme activity
What is the role of a prosthetic group in enzyme kinetics?
Facilitate catalytic activity as a tightly bound cofactor
Which enzyme regulation mechanism involves the use of metal cofactors?
Allosteric regulation
What is the primary function of deoxyadenosyl cobalamin in enzyme kinetics?
Facilitating methylmalonyl mutase activity
In enzyme kinetics, what is the main function of coenzyme A (CoA)?
Participating in acetyl group transfer reactions
How do metal cofactors contribute to enzyme kinetics?
Enhance catalytic activity by stabilizing enzyme-substrate complexes
What is the primary function of the digestive enzymes synthesized as zymogens in the stomach and pancreas?
Protein digestion
Which enzyme is responsible for converting pepsinogens to pepsins in the gastric lumen?
Pepsin
Which enzyme is NOT involved in the coagulation cascade for blood clotting?
Chymotrypsin
What is the role of procarboxypeptidases A and B in the pancreatic digestion process?
Hydrolysis of proteins
Which enzyme participates in the breakdown of triglycerides into free fatty acids during pancreatic digestion?
Pancreatic lipase
Which type of enzyme catalyzes the transfer of functional groups between different molecules?
Transferase
What is the function of Isomerases among the mentioned enzyme classifications?
Facilitate isomerization reactions within molecules
Which of the following enzymes is involved in joining two molecules together?
Ligase
Among the mentioned enzyme types, which one is primarily involved in catalyzing oxidation-reduction reactions?
Oxidoreductase
What is the main function of Hydrolases in biochemical reactions?
Catalyze removal of functional groups through hydrolysis reactions
What is the primary function of ligases in enzyme regulation mechanisms?
Catalyze the transfer of functional groups from one molecule to another
Which type of enzyme regulation involves irreversible activation of zymogens/proenzymes?
Hydrolases
How do isomerases contribute to enzyme regulation mechanisms?
Facilitate the conversion of substrates into their isomeric forms
In enzyme regulation, which group of enzymes undergo irreversible activation cascades?
Oxidoreductases
How do transferases contribute to regulating enzyme activity?
Catalyze the transfer of functional groups between molecules
Which type of enzymes are caspases, involved in programmed cell death?
Hydrolases
In apoptosis, caspases function to cause cell death by degrading proteins indiscriminately. What other enzymes share this indiscriminate degradation characteristic?
Ligases
What type of enzyme is procollagenase converted into during the metamorphosis of tadpoles into frogs?
Ligase
Which pathway can initiate apoptosis through the activation of caspases?
Intrinsic pathway
During apoptosis, what happens to the apoptotic bodies that are produced?
They are cleared by macrophages
What is the primary function of homotropic allosteric effectors on enzymes?
Enhance the catalytic properties of other substrate-binding sites
In covalent modification of enzymes, what is the primary role of kinases?
Catalyze the addition of phosphate groups to specific amino acids
Which term best describes an effector that is different from the substrate and influences enzyme activity?
Heterotropic effector
What is a classical example of heterotropic effectors in enzyme regulation?
Feedback inhibition in a metabolic pathway
How do positive homotropic effectors influence enzyme activity?
Enhance the catalytic properties at other sites
Which type of enzyme catalyzes the transfer of functional groups between molecules?
Transferases
What is the primary function of Ligases in cellular physiology?
Joining molecules together
Where do zymogens play a significant role in enzyme activation?
Golgi apparatus
What characteristic distinguishes Isomerases among other enzyme classes?
Catalyzing the interconversion of isomers
In what condition can accidental activation of zymogens prevent enzyme activity?
Blocked secretion duct in the pancreas
Test your knowledge on enzymes with this quiz covering cofactors, zymogens, apoptosis, and enzyme regulation mechanisms. Get ready to understand the physiological relevance of zymogens and the working of apoptosis. Ideal for students studying cellular biology and homeostasis.
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