In an enzyme, the allosteric site is a site/motif different from the active site, (i.e., the site with catalytic activity) which is able to interact with regulatory effector molecules in order to activate or inhibit enzymatic activity by influencing the tridimensional (3D) structure of the enzyme. An allosteric activator is an effector molecule with the ability to bind to a specific enzyme at a different site than the active site, thereby modifying the shape of the enzyme and increasing the affinity of this enzyme for its substrate. Moreover, Adenosine monophosphate (AMP) is a nucleotide composed of a phosphate group, a sugar ribose, and an Adenine (A) base. This effector molecule (AMP) has shown to allosterically stimulate diverse enzymes in physiological conditions (e.g., AMP-activated protein kinase).

5 0

2 years ago

True or false? alcohol has been found to increase one's risk for various types of unintentional injuries including drowning, fal

Viefleur [7K]

The answer is a. True

4 0

2 years ago

In the activity, you will balance two equations at each level: easy, medium, and hard. The equations to balance are listed below

vredina [299]

Easy:

1. 2K + Br2 — KBr

2. 4Sb + 3O2 — SB4 O6

Medium:

1. 2Na+2H2O — 2NaOH+H2

2. 2KNO3 — 3KNO2+O2

Hard:

1. 4NH3+5O2 — 4NO+6H2O

2. C2H5OH+3O2 — 2CO2+3H2O

6 0

2 years ago