In the structure of Alkaline Phosphatase enzyme what is the distance between the metal ion and the phosphate atom?, the distance between that metal ion and the PO32- group within the active site, what are the 3 amino acids that coordinate the metal ion in the active site of the enzyme?, other metal ion is located close to the zinc atoms.

In the structure of Alkaline Phosphatase enzyme what is the distance between the metal ion and the phosphate atom?, the distance between that metal ion and the PO32- group within the active site, what are the 3 amino acids that coordinate the metal ion in the active site of the enzyme?, other metal ion is located close to the zinc atoms.

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter19: The Tricarboxylic Acid Cycle

Section: Chapter Questions

Problem 23P

See similar textbooks

Similar questions

1. Requirements of Active Sites in Enzymes The active site of an enzyme usually consists of a pocket on the enzyme surface lined with amino acid side chains necessary to bind the substrate and catalyze its chemical transformation. Carboxypeptidase, which sequentially removes the carboxyl-terminal amino acid residues from its peptide substrates, consists of a síngle chain of 307 amino acids. The two essential catalytic groups in the active site are furnished by Arg45 and Glu²7º. (a) If the carboxpeptidase chain were a perfect a-helix, how far apart (in nanometers) would Arg'45 and Glu²7º be? Hint: In an æ-helix, there is 1.5 Å translation of the backbone per residue (Chapter 3). (b) Explain how it is that these two amino acids, so distantly separated in the sequence, can catalyze a reaction occurring in the space of a few tenths of a nanometer. (c) If only these two catalytic groups are involved in the mechanism of hydrolysis, why is it necessary for the enzyme to contain such a large…
Activity (% Max.) Using your knowledge of aspartyl proteases, develop a plausible explanation for why protein activity changes when pH is increased or decreased from pH 4, as shown in the graph. 06 08 09 10+ 4. 9. Hd Which statements are true? The protein is active when one asp residue is protonated and the other is deprotonated. O Both asp residues are protonated at more basic pH values. O Active aspartyl proteases have only one asp residue in the active site. Only one asp side chain is protonated at low pH (below pH 3.5). Both asp side chains are deprotonated at higher pH values.
Enzyme X exhibits maximum activity at pH- 6.3. X shows a fairly sharp decrease in its activity when the pH goes much lower than 5.8. One likely interpretation of this pH activity is that: a Glu residue on the enzyme is involved in the reaction. O the enzyme uses NADH has a cofactor the enzyme uses coenzyme A has a cofactor O a Tyr residue on the enzyme is involved in the reaction. O a His residue on the enzyme is involved in the reaction
AutoSave 301-Enzyme Kinetics and Inhibition, Part 3 - Compatibility Mode - Word Search ff steve M SM File Home Insert Draw Design Layout References Mailings Review View Help E Share O Comments prepared five different concentrations of substrate (sucrose), and five different concentrations of inhibitor C (plus the control, with zero mM of inhibitor C). The following Table lists the inhibitor C concentrations [I], substrate concentrations [S], and resulting enzyme velocities (V.) for all six of these experiments: [I] O mM O mM O mM O mM O mM [S] Vo 1/[S] 1/ Vo 0.1 mM 0.333333333333 mM per minute 0.2 mM 0.50 0.3 mM 0.60 0.4 mM 0.666666666667 0.5 mM 0.714285714286 0.1 mM 0.1 mM 0.166666666667 0.1 mM 0.2 mM 0.25 0.1 mM 0.3 mM 0.30 0.1 mM 0.4 mM 0.333333333333 0.1 mM 0.5 mM 0.357142857143 0.20 mM 0.1 mM 0.111111111111 0.20 mM 0.2 mM 0.166666666667 0.20 mM 0.3 mM 0.20 0.20 mM 0.4 mM 0.222222222222 0.20 mM 0.5 mM 0.238095238095 0.3 mM 0.1 mM 0.083333333333 0.3 mM 0.2 mM 0.125 0.3 mM 0.3 mM…
Shown below is a substrate for a Trypsin. Draw the mechanism for this serine protease using the artificial substrate. Be sure to draw the catalytic triad, and show the role of the oxyanion hole. Draw the complete structure of every intermediate and product and PUSH ARROWS!!!!! Do not abbreviate structures using R and R' H₂N _N_CH. сно CH₂ CH₂ CH₂ NH d=19H₂ NH₂ O CH- H₂C HN O CH
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
sapling learning (a) Identify the group in pyridoxal phosphate (PLP) that covalently binds enzyme and substrate. Hint A B _H OH Previous CH3 (b) Aminotransferases (transaminases) must deaminate one amino acid and add an amino group to another amino acid during transamination. How do the two processes differ? Map The 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 the removal of the amino group from the first amino acid. Give Up & View Solution Check Answer Next Exit
in human 2. Human xanthine oxidase catalyzes the oxidation of hypoxanthine to xanthine and can further catalyze the oxidation of xanthine to uric acid. For the treatment of hyperuricemia and gout. several medications are used to inhibit the activity of xanthine oxidase and reduce the production of uric acid. You are a biochemist and just discovered a chemical that can inhibit the activity of the human xanthine oxidase. When analyzing its mode of inhibition, you found that the enzyme inhibitor complex requires 450 kJ.mol to dissociate and that it displays kinetics somehow similar to noncompetitive inhibition. You sent your inhibitor to the ministry of health for approval as a medication for gout. Based on the data provided, are they going to authorize it as a medication or not? Explain?
Result nad Discussion Lead Acetate Reaction: Samples: lysine, cysteine, methionine Reagents: 10% Sodium Hydroxide (NaOH) and Lead Acetate Pb(CH3COO)2 -To 1 ml of the amino acid solution taken in a test tube, add few drops of sodium hydroxide (40%) and boil the contents for 5-10 mins over a bunsen burner. Cool the contents and add few drops of 10% Lead acetate solution and observe.
nment Score: 85.7% O Resources Lx Give Up? O Hint Check Answer on 13 of 23 > Attempt 4 The following tetrapeptide was digested completely with proteolytic enzymes. Modify the structure to show the amino acid hydrolysis products of this digestion, including the appropriate protonation and charge for each carboxyl and amino group at pH 7. Use the Erase tool to remove bonds where necessary. Select Draw Rings More Erase H H,N. CH, CH, CH, CH, OH acer
1. pH Effects a. In the enzyme mechanism of lysozyme, two acidic amino acid residues, Asp52 and Glu35, are critical for catalytic activity. If we assume normal side chain pKa values for Asp (pKar = 3.90) and for Glu (pKar = 4.07), what proportion of enzyme molecules will have both Asp52 and Glu35 in the correct ionization state at pH 5.0 (the pH optimum for lysozyme)? b. Are the traditional pKa values likely to be correct within the protein? What pKa changes might be present within lysozyme?
Activity, Enzyme Kinetics Biol 250, Spring 2022 The initial rate for an enzyme-catalyzed reaction has been determined at a number of substrate concentrations. Data are as follows: [S] (umol/L) V [(µmol/L) min1] 5 22 10 39 20 65 50 102 100 120 200 135 (a) Estimate Vmax and KM from a direct graph of v versus [S]. Do you find difficulties in getting clear answers? (b) Now use a Lineweaver-Burk plot to analyze the same data. Does this work better? (c) Finally, try an Eadie-Hofstee plot of the same data. (d) If the total enzyme concentration was 1 nmol/L, how many molecules of substrate can a molecule of enzyme process in each minute? (e) Calculate kcat/KM for the enzyme reaction. Is this a fairly efficient enzyme?