Pyruvate can be converted to acetyl-CoA by decarboxylation. Beta oxidation can convert fatty acids to acetyl-CoA. Transaminases can be used to make alpha-keto acids, which can be converted to acetyl-coA. Glucose cannot be directly converted to acetyl-CoA; it must be transformed into pyruvate first.

Carbohydrates can be stored as glycogen in the liver, fats can be stored as triglycerides or fatty acids in adipose tissue, and proteins can be made into alpha-keto acids. Hence, all of these are forms of energy storage that can be used as alternative energy sources.

Cellulose is a polysaccharide that is found in plants. Humans cannot digest cellulose due to its beta-glycosidic linkages.

The only option that will alter the is to add a non-competitive inhibitor. The addition of this inhibitor will affect the amount of free enzyme available to catalyze the reaction, and thus lower the by reducing the effective enzyme concentration.

Addition of a competitive inhibitor will alter the , but not the . Increasing the substrate concentration will have no effect once saturation has been reached. 

All of the given choices represent oxidation-reduction reactions that are important in cellular metabolism. Oxidation-reduction reactions involve the changing of oxidation states (commonly through the transfer of electrons). In the first reaction NAD⁺ is reduced. The second reaction shows the polymerization of two molecules of glucose via a condensation (dehydration synthesis) reaction. In the third reaction glucose is oxidized.

NADH and are important electron carriers that bring electrons to the electron transport chain and are formed during glycolysis and the Krebs cycle via reduction. The final choice represents the overall oxidation-reduction reaction that occurs for one molecule of glucose.

The induced fit model explains one method by which an enzyme's active site can accept some specific substrate. Initially, the active site might not be a perfect match for the substrate, however, when the substrate enters into the site, it can change the conformation of the enzyme just enough that it now fits perfectly and can be acted upon by the enzyme.

To answer this question, we need to have a general understanding about amino acid properties. For instance, at physiological pH, some amino acid side chains will carry a negative charge, some will carry a positive charge, and others will be neutral. Thus, we'll need to take note of which amino acid characteristics each position has, and then evaluate each answer choice to see if the new amino acid being substituted has different characteristics.

At position  is arginine, which carries a positive charge. At position  is valine, which has an aliphatic side chain that is neutral and relatively hydrophobic. At position  is the amino acid glutamate, which is negatively charged due to the carboxyl group on its side chain. Finally, we have glycine at position , which contains a lonely hydrogen atom as its side chain.

Now that we have the characteristics of the amino acid residues in the enzyme, let's compare them to the substitutions listed in the answer choices.

Substituting an aspartate residue into position  would mean replacing valine (neutral) with a positively charged amino acid. Hence, this would likely result in disruption of enzyme activity.

Substituting a tryptophan residue into position  would replace glycine. In contrast to the extremely small side chain of glycine, the side chain of tryptophan is very large. This great size discrepancy could potentially lead to steric effects that could interfere with the binding of substrate to the enzyme.

Substitution of an asparagine residue into position  would replace glutamate. Because glutamate is negatively charged, whereas asparagine is neutral, this substitution would likely interfere with enzyme activity.

Finally, let's consider the substitution of arginine at position  with a lysine. In this case, a positively charged arginine would be replaced by another positively charged amino acid, lysine. Because of the similarity between these two amino acids, this substitution would be the least likely to cause a disruption in the enzyme's activity.

A peptide bond is formed via the condensation of one amino acid's alpha-carboxy group with the alpha-amino group of another amino acid. Thus, the joining together of two amino acids results in the loss of one water molecule. Likewise, joining three amino acids together results in the loss of two water molecules. Following this pattern, we can conclude that the number of water molecules lost is equal to the number of amino acids joined together, minus 1. Therefore, the joining together of 100 amino acids results in the loss of 99 water molecules.

A peptide bond connects two amino acids. This is the result of a condensation reaction (water is lost) and a new nitrogen-carbon bond forms between two amino acids. Note that amino acid synthesis occurs in the  direction. Peptide bonds are covalent bonds that are responsible for the primary structure of amino acids.

For this question, we are presented with three different amino acids and are asked how many possible ways they can be arranged. One way to do this is to list out all the various ways they can be connected.

1) Gly-Leu-Glu

2) Gly-Glu-Leu

3) Leu-Gly-Glu

4) Leu-Glu-Gly

5) Glu-Leu-Gly

6) Glu-Gly-Leu

Alternatively, we could use the mathematic expression  to determine the number of combinations of three separate things, which is equal to .

The peptide bond within a polypeptide creates planarity, while other parts of the polypeptide are free to rotate. This occurs because of a delocalization of the electrons on the nitrogen of the amino group (resonance), forming a partial double bond.

While there is a slight difference in electronegativity between carbon and nitrogen, this does not effect the planarity of a polypeptide. Additionally, while a small and insignificant amount of hydrogen bonding may occur between side chains and water, it would not effect planarity regardless.