sapling learning(a) Identify the group in pyridoxal phosphate (PLP) that covalently binds enzyme and substrate.HintAB_HOHPreviousCH3(b) Aminotransferases (transaminases) must deaminate one amino acid and add an amino group to anotheramino acid during transamination. How do the two processes differ?MapThe second part of the reaction (adding an amino group) is the reverse of the first (deamination).The second part of the reaction takes place at a separate amino acid residue in the active site.The first reaction involves the formation of a Schiff base, whereas the second does not.The coenzyme PLP must be activated by an external amino group before it can catalyze theremoval of the amino group from the first amino acid.Give Up & View Solution Check Answer NextExit

PLP (pyridoxal phosphate):It is the active form of vitamin B6 i.e., a water-soluble vitamin which is…

Answered: Aminotransferases (transaminases) amino…

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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Reminder: Enzymology is foundational to biochemistry. You should review and be familiar with the enzymes unit from BICH410. Here is a sample question as review!! Which of the following characteristics is(are) accurate in describing a regulated enzyme? Select all that apply. a) always responds the environment by covalent modification by phosphorylation b) displays only negative cooperativity c) contains multiple subunits d)has a defined T state and R state
A substrate is converted to a product via the reaction sequence (1) E +S ES k2 (2) ES + S ES2 k4 (3) ES2 ES +P (4) ES , E +P (a). Using pseudo-steady state hypothesis for various forms of enzyme active sites, obtain relations between rates of individual steps in the mechanism. (b). Relating concentrations of vacant active sites to concentrations of occupied active sites, obtain expressions for the rate of consumption of S, (-Rs), and the rate of formation of P, Rp. (c). What are the maximum values of (-Rs) and Rp and under which conditions are these attained?
Practice Mira Gendy 1 of 1 Directions: This short free-response question requires about 6 minutes to answer. The question is worth 3 points. Read the question carefully and completely. Answers must be written out in paragraph form. Outlines, bulleted lists, or diagrams alone are not acceptable. II Substrate Concentration [S] The graph above shows the initial rate of an enzyme-catalyzed reaction at different substrate concentrations in the presence of a constant concentration of the enzyme. Connect the primary structure of the enzyme to its overall shape. I U x X2 5 Initial Rate of Reaction
. The optimal conditions for salivary lysozyme (hydrolyzing glycoproteins of bacterial wall) are 37 C - temperature and pH is 5.2. Explain the decrease in this enzyme activity if the temperature will rise up to 60 °C and pH will be changed to 8.0. To answer the question: a) draw the graph of the velocity dependency on temperature and pH; b) calculate the relative enzyme activity if 10 mg of lysozyme catalyzes the formation of 5 uM of the product per 2 minutes. Concidor NH3: 5.
Using the acromyn LILHOT give the 6 major families of enzymes found in biological systems. Describe the enzymatic activity of the "I" in LILHOT
Let’s consider vmax. Recall that uncompetitive inhibitors bind to the enzyme only after thesubstate is bound.a) As the concentration of substrate increases, the fraction of enzyme bound to substrate (circleone) increases / decreases?b) Does an uncompetitive inhibitor bind more readily when the substrate concentration is low orhigh?
Inhibitor X exerts which of the following effects on the above enzyme (maltase)? (inhibitor X changes maltase activity to a V o of 0.10 mM per minute when [S] = 0.125 mM, and a V o of 0.25 mM per minute when [S] = 0.50 mM)
protease mechanism: you isolate a new protease which cleaves the peptide bond 2 aa residues before a F residue. You might expect to fınd... O An I residue in the S2'pocket AL residue in the S2 pocket O aV residue in the oxyanion hole An Lresidue in the catalytic triad in Michaelis-Menton kinetics, cutting the enzyme concentration in half will O will double the reaction rate O will not change Vo and Vmax will change Vo but not turnover number decrease Km by half
. Propose a chemical mechanism for the reaction catalyzed by the PLP-dependent glatamate 1-semialdehyde aminomutase.
Blue numbers (3, 10, 11, 14, 16, 17) refer to a biochemical molecule Orange numbers (1, 2, 5, 6, 7, 8, 9, 12, 15) refer to reaction(s) in the pathway/process.Black numbers (4, 13 ) refer to an entire pathwayEach arrow may indicate multiple biochemical reactions required Match the description of lipid metabolism to the number on the figure (1-17): Inhibits b-hydroxy-b-methylglutaryl reductase Produced during the oxidation of malate to pyruvate…
1B. please help me in detail. Draw a graph of free energy G (y-axis) vs reaction progress (x-axis) that illustrates what the kinase is doing in terms of the free energy by showing (i) the substrate (also label what the substrate is [it’s name]), (ii) the products (also give the name of the products), (iii) draw and label the uncatalyzed and catalyzed reactions, and be sure that the parts of the graph are properly labeled..
Explain and differentiate the lock-and-key and induced fit models for binding of a substrate to an enzyme. If only a few of the amino acid residues of an enzyme are involved in its catalytic activity, then why does the enzyme need such a large number of amino acids?

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Aminotransferases (transaminases) amino acid during transamination