Answer:
(B) They may have binding sites for regulatory molecules that are separate from active sites.
(C) They generally have more than one subunit.
(E) They interconvert between a more active form and a less active form.
Explanation:
Allosteric enzymes are the regulatory enzymes that have a specific site for binding of modulator or effector molecule. The activity of these enzymes is altered by the noncovalent binding of modulators at the allosteric site. The binding of the modulator brings about a conformational change in the allosteric enzymes.
The relatively inactive conformation of these enzymes is called T state while the active conformation is the R state. Most of the allosteric enzymes have multiple subunits and deviate from Michaelis–Menten kinetics and exhibit a sigmoid saturation curve of V0 vs. [S].
Answer:
You drove through Iowa in the spring and noticed that along a stretch of several kilometers, every third fence post had a male red-winged blackbird perched on it defending its nesting territory. This is an example of <u>uniform dispersion.</u>
Explanation:
There are usually three dispersion patterns :
- Clumping
- Uniform dispersion
- Random dispersion
Clumping is the most common.
Uniform dispersion occurs when
- resources are scarce
- Individuals are evenly spaced in a habitat
- Due to competition or territorial behavior
While Random dispersion occurs when resources are plentiful.
Hence ,This is an example of <u>uniform dispersion.</u>
The neurons conduct impulses over relatively long distance in the body. This is facilitated by their long cytoplasmic extensions
Answer:
The correct answer is option c. "Enzyme lowers the activation energy".
Explanation:
The activation energy is defined as the amount of energy needed for a reaction to take place. Enzymes catalyze reactions by lowering the activation energy, which speeds up the reaction and increases its rate. Enzymes put a substrate in its active site, which facilitates the reaction and makes more likely that it collides with its subsequent substrate.
