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:mutualism
Explanation:
In a mutualistic relation,both organisms involved benefit from the activities of each other. The benefits may be nourishment,shelter, protection etc.
In the above example,the birds are known to guide humans by responding to specific calls made by the human. They guide humans to beehives and then in return gets to feed on left over honey. Both the bird and human benefits by getting nourishment.
Mutualism is unlike parasitism where one of the organism involved benefits and the other organisms Is most likely harmed. It is also not commensalism, where one organism benefits and the other neither benefits nor is harmed
Widened margins does not occur at the continental margin
Answer:
You tell her that this is incorrect.
Explanation:
The given information is incorrect as both small and large ribosomal subunits are required for protein synthesis. The eukaryotic ribosomes have E, P, and A sites. The A and P sites bind to the aminoacyl tRNA that carry the amino acid encoded by the codon of the mRNA.
The formation of peptide bond occurs between the amino group of amino acid in A site and the carboxyl group of amino acid present on P site. Both 40S and 60S subunit of ribosome contribute the A and P sites.
