How would the lock-and-key model explain that sucrase hydrolyzes sucrose, but not lactose?

If a blood test indicates a high level of ALT, what could be the cause?

How is the active site different from the whole enzyme structure?

After the products have formed, what happens to the enzyme?

How is the LDH isoenzyme in the heart different from the LDH isoenzyme in the liver?

What kind of interaction attracts the cofactor Mg²⁺ and ATP to each other? (Hint: Look at the structure of the phosphate group.)

Match the terms (1) active site, (2) lock-and-key model, and (3) induced-fit model with the following descriptions:

a. the portion of an enzyme where catalytic activity occurs

b. the active site adapts to the shape of a substrate

c. the active site has a rigid shape

Do the amino acids that are in the active site of an enzyme have to be near each other in the enzyme’s primary structure? If no, explain.