Below check question.Only a and b part solve ok Question 9Use the following information to answer Questions 9 andPart c.Consider the reduction of ribose to ribitiol bycatalytic hydrogenation, as shown below:HOOH OHOH OHBlank 1Blank 2H₂PtFor part a), respond to the question by entering anumber (ie 1, 2, 3, etc) into the blankHOFor part b), respond YES by entering Y into the blank,and NO by entering Na) How many chiral centres are present in ribose?Blank 1b) Is ribitol optically active? Blank 2Add your answerOHAdd your answerc) Drawing Ofanontiomer ofRiboseOH OHOH

There are four classes of biological macromolecules: proteins, nucleic acids, lipids and…

Answered: Question 9 Use the following…

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

Question 1: When the CAC is run in reverse by microorganisms that use it to fix carbon, the citrate synthase reaction is different and is catalyzed by an enzyme called ATP-citrate lyase. Write the reaction catalyzed by ATP-citrate lyase, then briefly (in one sentence) explain why the use of different chemistry (different from the ‘normal’ direction) makes sense here.
Question 1: The overall process enabled by the glyoxylate cycle is: (2acetyl-CoA) + (NAD+) + (2H2O) → (succinate) + (2CoA) + (NADH) + (2H+) Dissect this process further by writing down all of the reactions that are actually involved in making one succinate from two acetyl-CoA units. Show chemical structure for all intermediates.
QUESTION 22 When the final product of a series of enzymatically-catalyzed reactions binds to the first enzyme in the pathway to limit its production, it generally uses ___ because the structure of this final product is generally not similar to that of any of the enzyme's normal substrates. Allosteric activation Zymogen activation Covalent modification Competitive inhibition Allosteric inhibition
QUESTION 26 During gluconeogenesis, whereby liver cells convert pyruvate to glucose, Fructose-6-phosphate (F6P) is converted to Glucose-6-phosphate (G6P). If the standard equilibrium concentrations are: [F6P] = 0.52 M and [G6P] = 1.48 M, then Keq’ is ______ and the reaction is ________. Fructose-6-P ó Glucose-6-P > 1; exergonic > 1; endergonic < 1; exergonic < 1; endergonic
QUESTION 1 a. John has just taken his Lunch meal, after which he is going to takes his Daily soccer practice match in the next 30 min, how will glycolysis operate/work in such conditions or be applicable b. How will oxidative phosphorylation work in sickly John who usually practice daily in soccer? Make possible scenarios c. Enzymes are critical in the metabolism of most most organic compounds, actually 30% of reactions are catalysed by them. How would the inactive enzymes (Sickness) in electron Transport Chain compromise the fat breakdown in the body.
Question 1: The 4 kinase steps in glycolysis are catalyzed by hexokinase, phosphofructokinase, phosphoglycerate kinase, and pyruvate kinase. Write each of these four reactions, including all participants. i. ii. iii. iv.
QUESTION NO. 1Statements: (1) Glucose is both a hexose and a aldose. (2) There can never be more than three enantiomers for a molecule. (3) All common disaccharides have beta-one-four linkages. Which statements are true?QUESTION NO.2 Erythrocyte glucose transporter illustrates the type of A. ion driven active transport B. facilitated diffusion C. active transport D. simple diffusion E. secondary active transportQUESTION NO.3 which of the following statement/s accurately describe the surface of a lipid droplet? A. a monolayer of phospholipids B. a bilayer of phospholipid C. a network of perilipin protein D. a structured layer of triacylglycerol E. a chaotic hydrophobic/ hydrophilic interface
Question 1: The standard reduction potential for the the cytochrome c Fe3+/Fe2+ redox couple and for the dioxygen/water redox couple. Part a: Use these values, and the relevant equation, to compute the standard free energy change for the transfer of 4 electrons from cytochrome c to dioxygen. Part b: Next, compute the free energy needed to pump four protons across the mitochondrial membrane, using the relevant equation and values of -.14V for Δψ and 1.4 for ΔpH. Part c: If energy conservation by cytochrome c oxidase involved only the four pumped protons (and standard conditions applied), what would be the efficiency of energy conservation at this step? (what is the ratio [energy conserved in the gradient] / [redox energy used] ?)
Question 12 Carbohydrates that appear in glycosylated proteins and lipids in the GA include I. N-Acetylglucosamine II. fucose III. mannose IV. galactose I, II, IV only I, II, III only II, III, IV only I, II, III, IV
QUESTION 2An isocitrate dehydrogenase assay was performed on the enzyme sample and found to give an absorbance change at 340nm of 0.5 absorbance units perminute. Given that the molar absorption coefficient (E) is 6220 M-1 cm-1 and the pathlength is 1cm, what is the rate of the enzyme catalysed reaction in umol perminute per mL?
Question:- The enzyme aromatase is found in the cytoplasm of some cells and converts testosterone to estrogen. You decide to test aromatase from a particular cell, and oops, your lab partner admits he drastically increased the pH in all the test tubes. Which of the following is a likely result? a. The enzyme will be denatured and the substrate will not bind to the active site. b. The enzyme will convert testosterone to estrogen at a faster rate. c. The mistake will have no effect on the experiment, because enzymes are not sensitive to pH. d. The free energy will be lowered and the reaction will not proceed spontaneously.
Question 29 options: If 6 molecules of acetyl CoA were completely oxidized by the CAC, how many molecules of FADH2 would be produced?

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