Question

In allosteric regulation, effector molecules usually bind...

1) reversibly and covalently
2) irreversibly and covalently
3) reversibly and noncovalently
4) irreversibly and noncovalently

Answer 1

In allosteric regulation, effector molecules usually bind reversibly and noncovalently to the allosteric site of an enzyme, causing a conformational change that affects substrate binding and reaction rates.

Step-by-step explanation:

In allosteric regulation, effector molecules usually bind reversibly and noncovalently.

Allosteric regulation is a type of enzyme regulation where a molecule, called an effector, binds to a site on the enzyme called the allosteric site. This binding induces a conformational change in the enzyme, altering its active site and affecting substrate binding and reaction rates. The binding between the effector and the enzyme is reversible and usually occurs through noncovalent interactions.