18 Questions
What is the term used to describe enzymes that catalyze the same type of reaction but are created by different genes and have different molecular shapes?
Isoenzymes
Which term refers to an enzyme that combines with only one substrate and catalyzes only the one corresponding reaction?
Absolute Specificity
What is a coenzyme where a cofactor is bound tightly to an enzyme referred to as?
Prosthetic Group
Which term describes the inactive form of an enzyme that needs to be activated?
Proenzyme
In the Enzyme Commission (EC) code number, which digits represent the subclass and sub-subclass of the enzyme?
Second and third digits
What do you call an active system composed of a prosthetic group and an apoenzyme?
Holoenzyme
What is the main difference between isoenzymes?
Varying molecular structure
How do non-competitive inhibitors differ from competitive inhibitors?
They bind to areas other than the active site
What is a characteristic of a non-competitive inhibitor?
Binds independently from the substrate
How does storage at low temperatures affect enzymes?
Preserves enzyme activity reversibly
What is a key aspect of fractionating isoenzymes?
Enhancing total enzyme activity
Why is non-competitive inhibition considered allosteric?
It binds to areas other than the active site
What is the role of the allosteric site in an enzyme?
It binds regulator molecules and influences the enzyme structure
Which type of enzyme catalyzes the transfer of a group other than hydrogen from one substrate to another?
Transferases
What do Hydrolases catalyze in terms of bond breaking?
Hydrolysis of various bonds
How do Lyases catalyze the removal of groups from substrates?
Without hydrolysis, forming products with double bonds
Which class of enzymes catalyze the interconversion of isomers?
Isomerases
What does an abnormally large amount of enzymes in the serum usually indicate?
Organ damage
Test your knowledge on isoenzymes, enzymes with the same catalytic reactions but slightly different molecular structures, and non-competitive inhibitors. Learn about how isoenzymes can have various forms due to differences in amino acid sequences and how non-competitive inhibitors do not compete with substrates.
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