Answer:
Yes, amylase can be reused, and when fulfills its catalytic function, it is free to catalyze the breakdown of another starch molecule.
Explanation:
Amylase is an enzyme capable of catalyzing the breakdown of starch bonds, separating it into glucose molecules.
The enzymes, including amylase, have the property of being free and without structural alteration when catalyzing a reaction, to bind to the specific substrate and catalyze a new reaction.
Amylase is not consumed, unlike a reagent, so it can be reused in new reactions.
Porosity
Porosity refers to the space inside the rock that is taken up by pore space.
Provided that there's no diagram, most molecules have particular areas on the molecules, called the "active area" that act as a lock to a particular substrate's molecular structure, providing the key.
An enzyme's active area is only able to be "unlocked" by a certain substrate's "key".
Answer:
maybe
Explanation: both idk for sure sry i tried
The correct answer is the last statement.
If the regulatory serine is mutated to alanine, then acetyl-CoA carboxylase will get activated spontaneously and will produce malonyl-CoA. The increased concentrations of malonyl-CoA will obstruct the oxidation of fatty acids by preventing the entry of fatty acids into the mitochondria.
It is because the AMP-activated protein kinase phosphorylates the serine residues of acetyl-CoA carboxylase to inactivate it. If a mutation occurs in such residues, then the AMPL cannot phosphorylate acetyl-CoA carboxylase and this enzyme will get activated spontaneously.
In such a situation, there will be more than sufficient production of malonyl-CoA, which will inhibit the admittance of more fatty acid getting inside the mitochondria; this will indirectly prevent the oxidation of fatty acids.
