Image A biosynthetic pathway for the synthesis of two molecules, E or H, from molecule A is shown below. Letters A through Hrepresent molecules, and numbers 1 through 7 represent enzymes. Observe that after the formation of molecule C, eithermolecule E or H can be formed depending on which pathway is followed. Note that if a build up of molecule H occurs at a highenough concentration, it impedes the action of enzyme 5 (that is what the curve to flat lines indicate).1 2 3 D4EB2A BA. What is the original reactant in the above pathways? [Select]5 F 6 G7 HB. Name an intermediate product in the pathway from molecule A to molecule E. [Select]C. Name an intermediate product in the pathway from molecule C to molecule H.D. Name a final product of this pathway.[Select]+F. Will the synthesis of molecule H then increase (1) or decrease (D)? [Select]E. If there is a high concentration of molecule E, which enzyme will be inhibited? [Select]G. What type of enzyme regulation is this an example of? [Select.][Select]→+

Enzymes can e reversibly inhibited in presence of competitive and non-competitive inhibitors. Such…

Answered: A biosynthetic pathway for the…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Lysozyme is an enzyme that hydrolyzes bacterial cell wall polysaccharides. When this reaction is carried out in the presence of H218O, it is observed that there is retention of configuration at the C1 carbon of the D site sugar as shown below: Would this result suggest that the enzyme mechanism involves the direct nucleophilic attack of water at C1 or that the enzyme mechanism involves attack by a nucleophilic amino acid side chain of the enzyme that generates a transient covalent intermediate?
PLP is a cofactor for a number of enzymes involved in amino acid metabolism. Give an example of reaction in which PLP participates in cleavage of the a, b, and c bonds of an amino acid, as diagrammed in shown Fig.
Which folate structure (from the list below)(a) is the substrate for the enzyme that is inhibited by methotrexate andtrimethoprim?(b) has the most highly oxidized one-carbon substituent?(c) is used in the conversion of serine to glycine?(d) transfers its one-carbon substituent to a B12 coenzyme? What amino acid is synthesized as the end result of this reaction?(e) is the coenzyme for the thymidylate synthase reaction?(f) is not known to exist in nature?(g) is used in purine nucleotide synthesis?
The diagram below shows an outline of the aminotransferase mechanism that skips the specific steps that show how electrons flow when a Schiff base is formed or is hydrolyzed. Using the mechanistic details given below A. Draw the mechanism for Enzyme- PLP Schiff base formation using pyridoxal and the lysine amine group using arrow to indicate electron flow. B.Draw the mechanism for hydrolysis of the Schiff base to form the a-keto acid, which is the reverse of the first reaction.
Trypsin, a peptidase that hydrolyzes polypeptides, functions in the small intestine at an optimum pH of 7.7–8.0. How is the rate of a trypsin-catalyzed reaction affected by each of the following conditions?
The active site of an enzyme that uses a general acid-base catalytic mechanism contains a Glu and an Asp residue (both of which are essential for catalysis) with pKa values of 5.9 and 4.5, respectively. If the enzyme is found in the lysosome (pH = 5.2), which residue will act as the general acid and which will act as the general base during the initial steps of the reaction?
The M and H subunits of lactate dehydrogenase have very similar sizes and shapes but differ in amino acidcomposition. If the only difference between the two were that theH subunit had a glutamic acid in a position where the M subunithad a serine, how would the five isozymes of LDH separate on electrophoresis using a gel at pH 8.6?
Why might the compound shown below act as a transition state analog of phosphoglucose isomerase? A drawing of the normal transition state for this enzyme is needed.
In a particular enzyme, an alanine residue is located in a cleft where the substrate binds. A mutation that changes this residue to glycine has little effect on activity; however, another mutation, which changes the alanine to a glutamate residue, leads to a complete loss of activity. Provide a brief explanation for these observations. As a follow-up on the previous question, you have another enzyme that you suspect binds its substrate in a similar site as the enzyme you are studying above. Assuming you have access to techniques whereby you could synthesize mutant proteins, outline experimental steps you would use to help you determine whether the two proteins recognize substrate by similar structural features.
a) Based on the mechanism shown in Figure 2A, what type of enzyme is transpeptidase? : Lyase Isomerase Ligase Hydrolase Oxidoreductase Transferase b) Transpeptidases have two substrates. From Figure 2A, what type of mechanism do they most likely adopt in processing the two substrates? sequential or ping-pong c) β-lactams inactivate transpeptidases by forming a covalent bond with the serine residue in the active site. Based on this description and Figure 2B caption, what type of inhibitor are β-lactams? _________________________________________ d) Based on the mechanism for lactamase shown in Figure 3, what type of enzyme is lactamase? Lyase Isomerase Ligase Hydrolase Oxidoreductase Transferase e) Based on your answer in d, what other reactant, in addition to the antibiotic substrate, needs to be in the active site of lactamase for the hydrolysis reaction to proceed? ____________________
Using the catalytic mechanism of serine proteases, draw and label a reaction coordinate diagram/graph of the chymotrypsin-catalyzed hydrolysis of a peptide bond.
Bacterial species that are capable of synthesising the amino acid histidine do not need it in their growth medium. Histidine biosynthesis requires a specific enzyme, which we shall refer to as histidine synthetase. When these bacteria are supplemented with histidine in their growth media, they cease intracellular histidine synthesis. Propose three distinct regulatory mechanisms to account for why histidine production ends when histidine is present in the growth medium. To further investigate this phenomena, you analyse the quantity of intracellular histidine synthetase protein produced when cells are cultured with and without histidine. The quantity of this protein is same in both scenarios. Which regulatory mechanism makes sense in light of this observation?

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