**Transcription for Educational Website:****Understanding Enzyme Functionality:**In most enzymes, the required active site amino acids consist of only a few residues. Why is the rest of the protein necessary for full enzyme function?- ○ To bind to the membrane through hydrophobic residues.- ○ To interact with other proteins so that the enzyme can be imported into the endoplasmic reticulum where enzymes are the most active.- ○ To provide the correct tertiary structure for the substrate binding site and for proper orientation of the catalytic residues.- ○ To provide protein targeting sequences so that the enzyme can be transported to the mitochondrial matrix where gluconeogenesis takes place.

Enzymes are proteins that function as biocatalysts and catalyse biochemical reactions.They have a…

Answered: In most enzymes, the required active…

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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Consider the metabolic pathway show below that converts substrate A to B with the enzyme A-ase, B to C with B-ase(I), and so forth. Acety/A-ase Acetate - A-ase Deacetylase A-ase Protease & C-ase B-ase ABCD What is the mechanism of regulation of B-ase? Positive allostery Reversible Covalent modification Isoenzymes Proteolytic Activation Feedback Inhibition 1
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Which of the following statement is FALSE ? pKa values of active site residues can be shifted from typical pKa values Enzymes increase Keq Near attack complexes have reacting molecules close enough to form Va der Waals contacts The transition state contains at least one partial bond. QUESTION 12 The angle o in a peptide best describes: O the angle between the two peptide bonds O the angle between the alpha carbon (Ca) and the amide O the angle between the alpha carbon (Ca) and the carbonyl O the angle between the alpha carbon (Ca) and its side chain QUESTION 13 Investigating how protein subunits come together studies: super- secondary structure Click Save and Submit to save and submit. Click Save All Ansuers to save all anscers 7977 Mostly cloody
A) Myth: Enzymes are specific for one substrate. Fact: Like most enzymes, alliinase can act on multiple different substrates. Explain why most enzymes can act on more than one substrate compound. (Refer to the “Alliin-like Substrates" panel in your answer.)
(c) On the right is a diagram of the ac tive site of E. coli aspartate aminotrans- ferase illustrating the cofactor pyridoxal phosphate (labeled PLP) with the dicar- boxylic acid maleate (labeled MAL) bound in the active site. The structural formula of maleate is shown on the right. Am 194 MAL Arg292 Arg386 Ilx17 Lauf 'coo- H get H Coo- Maleate (c1) Draw the structure of L-aspartate and draw a border around the atoms in the amino acid that maleate simulates. (c2) Identify the active site residues that make hydrogen bonds and electrostatic interac- tions with the oxygen atoms of the carboxylate groups of maleate in the diagram above. Identify the carboxylate groups according to the numbering in the diagram of maleate above. Indicate the hydrogen donor groups of the active site residues. (C3) Compare and draw the structures of L-Arg and L-Lys. On the basis of the diagram why does replacement of an arginine for a lysine have an effect on substrate binding to AspAT? (c4) Of the mutant…
The active site of an enzyme has a serine residue (shown below). Which of the following describes the substrate? H2N- CH- -OH OH polar active site, interacting atoms in substrate could be C-H Ononpolar active site, interacting atoms in substrate could be C-H polar active site, interacting atoms in substrate could be N-H nonpolar active site, interacting atoms in substrate could be N-H
Esterase hydrolyzes ester bonds. For simplicity, only the amino acids whose side-chains interact with the substrate are shown. Each circled interaction is important for the binding of the substrate to the enzyme. substrate x CH H-O CH3 CH Z CH, H,C CH, Esterase active site (a) Which of the above amino acids, (X, Y or Z) is closest to the N terminus of the primary sequence of the enzyme? (b) You create two mutants (1 & 2) of the enzyme, each of which has two amino acid substitutions at the active (substrate-binding) site. You observe that one mutant can bind to the substrate similarly to the wild-type version of the enzyme, whereas the other cannot. Which of the two mutant versions (1 or 2) will probably not bind to the substrate? Explain, in terms of the characteristics of amino acids, why you selected this version. Enzyme Wild-type Amino acids at the active site X Y Mutant 1 Asp Y Tyr Mutant 2 X Ala Ser
Concerning enzymatic activity, a larger Km value indicates a/an: Select one: O lower affinity for its substrate O inhibitory process O larger enzyme O larger Vmax O greater affinity for the substrate Which is the least common type of chemical bond? Select one: O Hydrogen O Peptide O Covalent O lonic O Disulphide D-gluconic acid is: Select one: O an integral membrane protein O a codon O an oxidized sugar O phosphorylated O a large lipid molecule
Changing which pairs of the amino acids is most likely to directly lead to the most severe problems with substrate (Blue) binding by the protein depicted by the red ribbon.
Small molecules are used as inhibitors of protein action - as drugs. They most often do this by blocking the active site within the protein. Potential drugs can be screened computationally to determine if they are strongly bound to the protein. Figure 1 shows a possible conformation of a candidate drug molecule, 4-bromo-2- carboxymethylamide-pyrrole (abbreviation: BCMAP) at the active site of a protein (abbreviation: PR). Figure 2 shows the full protein structure whilst figure 3 shows a known inhibitor of the protein at the site, overlayed with another calculated conformer of BCMAP. (a) Explain what types of interactions, both intermolecular and intramolecular, that a molecular mechanics forcefield must be able to describe in order to be able to accurately determine the geometry of BCMAP in the protein. Identify which interactions will be the most important to describe accurately. Figure 1.4-bromo-2-carboxymethylamide-pyrrole (BCMAP) (C, N, O, and Br atoms in yellow, blue, red, and…
The biosynthetic pathway for the two amino acides E and H is shown schematically in the Figure below: A W E 2 Z H How would this pathway change if C was mutated and non-functional?
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