Figure 1.+ΗNaOH, H2O (pKa = 15)heatH+"ДаHApKa = 20BpKa = 17DThe aldol condensation reaction in Figure 1 is an amazing example of how unfavorable equilibrium processes can bemanipulated to generate product in good yields. In this case, the major product is the self-condensation product, D. Thenext most abundant product is the crossed aldol product, C. There are 2 other less favorable products that could form butare not shown in Figure 1.Draw a plausible electron pushing mechanism to show how product C is formed. Remember, if analow Stans mom an electron pair, you must explicitly draw those electrons in.

Answered: Image /qna-images/answer/4a55e5c5-f918-4198-ab47-561657a83802.jpg

Answered: Figure 1. + Η NaOH, H2O (pKa = 15) heat…

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

See similar textbooks

Similar questions

Table 4. Rates of saponification at 35°C. Ester k(M-' sec") k, relative* (CH,O),PO, 2.0 x 10 3.4 x 10-4 1.0 x 10-2 1.0 2 x 10 5 x 10 CH,CO,C,H, "Rate relative to that of (CH,O);PO;". Question 3 Table 4 lists the rates of base catalyzed hydrolysis (saponification) for several different esters. Using your understanding of nucleic acids chemistry, explain why hydrolysis of the phosphodiester is slow compared to the phosphotriester and ethyl ester.
i) Re-arrange the Michaelis Menten equation so it involves the ratio [S]. Show all steps beginning Km noting any assumptions or required conditions. Km ii) Calculate the ratio [lo for the case when the rate of product formation is 68% of Vmax and the substrate is in great excess. d[P] dt : k₂ with = [E],[S] Km+[S]' [S]o Km iii) Explain, in a few sentences, why the ratio determines the ratio V Vmax V Vmax Begin by explaining the meaning of stating simply "it's the ratio...." is not sufficient. Include in your explanation the factors that effect v and Vmax. Consider what factors make v different from or equal to Vmax. Consider what Km represents concerning processes involving ES. " iv) Calculate KM at 310K at given the following rate constant information: k₁ = 17 s-¹M-1 at 300K with A = 7300 s-¹M-1 K-1₁ 6 s¹ at 300K with A = 14500 s -1 k₂ = 31 s¹ at 300K with A = 600 s-¹
Draw the major product of the following Suzuki coupling reaction. CN B(OH)2 CI 2 eq K₂CO₂ aq. 3 mol-% Pd(PPh3)4 benzene, A CI Draw the major product of the following Stille coupling reaction. OMe N Bu3Sn + Pd(PPh3)2Cl2 OAC THF, reflux
Explain the mechanism of this aldol condensation mechanism.
Match the following catalytic strategies with their example. Place a Letter on the picture. There are only two examples given. CH2OH CH2OH CH2OH CH2OH он он OH OH + H20 OH OH OH но H. но но OH OH OH OH OH OH A. Oxidoreducatase B. Transferase C. Hydrolase D. Lyase NH3 E. Isomerase F. Ligase R-CH-COO "ooc-CH2-CH2-C-COO Amino acid a-Ketoglutarate
16) The graph at right shows the results of reaction rate vs. substrate concentration for a Michaelis-Menten type enzyme a. True b. False 17) The equilibrium constant for the conversion of the disaccharide sucrose to the simple sugars glucose and fructose is 140.000 reaction rate->
Match the following catalytic strategies with their example. Place a Letter on the picture. There are only two examples given. CH2OH CH2OH H. CH,OH CH2OH он он OH Kon + H2O OH HO OH OH OH HO но OH OH OH OH A. Oxidoreducatase OH OH B. Transferase C. Hydrolase D. Lyase NH3 E. Isomerase F. Ligase R-CH-COO + 00C-CH2-CH2-C-COO Amino acid a-Ketoglutarate NH3 + 00c-CH2-CH2–CH-C0 R-C-COO a-Keto acid Glutamate
Carbonic anhydrase catalyzes the hydration of CO. CO2 + H2O ¬ H½CO3 The Km of this enzyme for CO, is 1.20×104 µ.M. When [CO,] = 3.60×104 µM, the rate of reaction was 4.50 umol·mL! sec-1 a What is Vmax for this enzyme? umol·mL-!sec-!
Please don't provide handwritten solution ....
when saturated with substrate, an enzyme has a maximum initial rate of 110mumoles of substrate converted to product per second. At a substrate concentration of 100mu M, the same enzyme converts substrate to product at a rate of 0.010mmoles/ sec. Assuming that Michaelis - Menten kinetics are followed, calculate the reaction rate when substrate concentration is 2x10^-3M.
Bacterial aldolase does not form a Schiff base with the substrate. Instead, it has a divalent Zn2+ ion in the active site. How does the ion facilitate the aldolase reaction?
Which of the following statements are False?

SEE MORE QUESTIONS

Recommended textbooks for you

Biochemistry

ISBN:

9781319114671

Author:

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

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781319114671

Author:

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

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781305961135

Author:

Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Publisher:

Cengage Learning

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Fundamentals of General, Organic, and Biological …

Biochemistry

ISBN:

9780134015187

Author:

John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson

Publisher:

PEARSON

SEE MORE TEXTBOOKS