19 Questions
Which of the following measures the speed of P formation once ES has been made?
Kcat
What does Kcat/Km measure?
Enzyme efficiency
What are some applications of enzyme inhibition?
Clinical therapies
What type of inhibition is reversible and involves competitive binding of the inhibitor to the active site of the enzyme?
Reversible inhibition
What is an example of a competitive inhibitor?
Methotrexate
In competitive inhibition, does Vmax change?
No
In uncompetitive inhibition, is Vmax lower or higher?
Lower
What happens in irreversible enzyme inhibition?
An inhibitor forms a covalent bond with the active site of the enzyme
What happens when an activator binds to a multi-subunit allosteric enzyme?
Enhances binding of the substrate to other subunits
Which enzyme has a lower Vmax and lower Km compared to glucokinase?
Hexokinase
What turns off hexokinase?
High concentrations of glucose-6-P
Where is glucokinase predominantly found?
Liver
Why can't other tissues convert excess glucose to glycogen?
They lack glucokinase
What is the significance of adding a phosphate group to glucose?
It traps glucose inside the cell
Which pathway is used for energy when glucose levels are low?
Glycolysis
What does high Vmax indicate?
High capacity to convert substrate to product
What is the role of aldehyde dehydrogenase?
Converts acetaldehyde to acetate
Why is hexokinase inhibited by glucose-6-P, but glucokinase is not?
Different regulatory mechanisms
What does a lower Km indicate?
Higher affinity for substrate
Test your understanding of the application of Km and Vmax in the metabolism of NAD+, ethanol, and acetate. Learn how alcohol consumption affects the conversion of NAD+ to NADH and the subsequent production of acetaldehyde and acetate. Explore the differences between glucokinase and hexokinase in terms of their Vmax and Km values.
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