Given what we know, we can confirm that if further increases in substrate concentration do not result in further increases in reaction rate, then an enzyme is likely saturated.
<h3>What does it mean for an enzyme to be saturated?</h3>
Enzymes work by binding to the substrate in specific zones of the enzyme. The zones are known as the active sites on enzymes. Since enzymes have a limited amount of these zones, once they are all bonded to a substrate, we can say that it is saturated.
Therefore, the saturation of enzymes allows us to explain how further increases in substrate concentration do not result in further increases in reaction rate.
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Answer:
The carbons of the acetyl group oxidize which generate CO2, and in turn H2O.
Explanation:
The pyruvic acid that is generated during glycolysis enters the mitochondria. Inside this organelle, the acid molecules undergo a process called oxidative decaborxylation in which an enzyme of several cofactors is involved, one of which is coenzyme A. Pyruvic acid is transformed into an acetyl molecule and these are been introduced to the begining of the Krebs Cycle where the acetyl-group (2C) from acetyl-CoA is transferred to oxaloacetate (4C) to produce citrate (6C). As the molecule cycles the two carbons of the acetyl oxidize and are released in the form of CO2. Then the energy of the Krebs cycle becomes sufficient to reduce three NAD +, which means that three NADH molecules are formed. Although a small portion of energy is used to generate ATP, most of it is used to reduce not only the NAD + but also the FAD which, if oxidized, passes to its reduced state, FADH2
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