7. Fill in the blank with the correct terms.Phosphorylation and dephosphorylation are what type ofenzyme regulation methods?а.Type of non-permanent enzyme inhibition that does notdirectly interfere with the enzymes active site.Class of enzyme that hydrolyzes esters, amides, andphosphoesters.C.Name of an enzyme that would catalyze the removal ofhydrogen from alcohols (product would be an aldehyde).d.Rank the energy bearing phosphate compounds AMP, ATP, andADP from the citric acid cycle in order of highest energy to lowest.b.e.

Introduction: Enzymes are biological catalysts that mean they are catalysts of life that increase…

Answered: 7. Fill in the blank with the correct…

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

I. Indicate whether each of the following statements are true or false. _1. According to the lock-and-key model of enzyme action, the active site of an enzyme is flexible in shape. 2. In an enzyme-catalyzed reaction, the compound that undergoes a chemical change is called the substrate. 3. The nonprotein portion of a conjugated enzyme is the enzyme's active site. _4. Simple enzymes have inorganic cofactors, and conjugated enzymes have organic cofactors. 5. Vitamins are required in minute quantities for normal cellular function. 6. vitamins are found in all food groups. 7. Ribose sugars are found on one chain of the DNA molecule and deoxyribose sugars are found on the other chain of the DNA molecule. 8. A DNA molecule has a double helix at one end of the molecule and a single helix at the other end of the molecule. _9. Complementary bases are held together by covalent bonds. 10. DNA molecules always contain the nitrogenous base thymine.
What are the effects of different light colors in photosynthesis? Different light colors will change the rate of photosynthesis Light color does not affect photosynthesis Carbohydrates are metabolized by light Photosynthesis does not require light
8. In patients with diabetes mellitus type 1, the biochemical disorders result from changes in fuel metabolism. One of these signs is acidosis, Explain why such patients have a deviation of blood pH from the norm? For this 9. b) write the reactions of synthesis and oxidation of these molecules, name the enzymes, coenzymes, reaction localization: X
The following statements refer to enzyme inhibition. Match the statement to the one of the following descriptors to which it is best associated. Descriptors: competitive inhibition; non-competitive inhibition; un-competitive; covalent inhibition. 9a. Inhibition is not reversed even after the inhibitor (1) is removed from solution by dialysis or drug metabolism/excretion. 9b. Inhibitor and substrate reversibly compete for occupancy of a common binding site 9c. The inhibitor binds reversibly only to the preformed E.S (enzyme-substrate) complex forming an inactive E.S.I. 9d. The inhibitor binds reversibly and independently of substrate to an allosteric site producing E.I or a ternary E.S.I complex which can't form product. 9f. The relative amount of inhibition decreases as [S] (the concentration of substrate) increases and S better competes for occupancy of the active site.
H8. Glucose labeled with 14 C at C-1 is added to a solution containing the enzymes and cofactors of the oxidative phase of the pentose phosphate pathway (aka hexose monophosphate pathway) which compounds will contain radioactive carbon? - Ribulose 5 phosphate, no label will be found, all compounds will be labeled, erythrose 4- phosphate, 7-[hps[hpsedoheptulose, fructose 6- phosphate, grlyceraldehyde 3-phosphate, xylulose 5 phosphate ribose 5 phosphate
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. Acetyl A-ase Acetate A-ase Deacetylase A-ase B-ase ABC- Isoenzymes Protease Inhibition What is the mechanism of regulation of A-ase? Reversible Covalent modification Isoenzymes What is the mechanism of regulation of A-ase? C-ase Reversible Covalent modification Proteolytic Activation Feedback Inhibition Positive allostery
A. Give a systematic name for the enzyme that would act on each of the following substrates 1. Methylamine 2. Glucose-6-Phosphate 3. Citrate 4. Glucocerebroside 5. Hydrogen peroxide
Refer to the figure. Portions of three biosynthetic pathways regulated through feedback inhibition and activation are shown. Two of these pathways intersect at carbamoyl phosphate. The third pathway generates a product that activates production of carbamoyl phosphate through allosteric modification of the enzyme carbamoyl phosphate synthetase. Arginine pathway Pyrimidine pathway Glutamate СТР Purine pathway N-acetylglutamate synthetase N-acetylglutamate UMP UMP ATCase Ornithine СР CO, + ATP Carbamoyl phosphate synthetase + Gin t-Arginine In this set of pathways, arginine biosynthesis is shut down through feedback inhibition when and arginine reach high levels of concentration. О СТР O ornithine O UMP O carbamoyl phosphate O glutamate
5. You discover a new cysteine protease similar to papain. Cysteine proteases are proteolytic enzymes that utilize a cysteine residue in the active site for the nucleophilic attack of a peptide bond, while a second residue acts as a base for proton abstraction in the reaction (acid base catalysis). In this novel enzyme the pKa of the cysteine residue is significantly lowered by the active site environment to pKa=4. a. Knowing that the protease shows highest activity between pH 4-6, what could be the identity of the base residue acting as a in the reaction? Explain and write the expected mechanism for the reaction. SH он
3. b. If chymotrypsin is treated with disopropylfluorophosphate, catalysis cannot occur even in the presence of excess substrate concentration. Is this Inhibltion reversible or Irreversible?. Dilsopropylfluorophosphate Hyd
C. running the reaction at 70 What are the functions of Allosteric enzymes What are some factors that affects enzyme activity? I. II. III. IV. V. VI. Enzyme activity can be regulated by allosteric enzymes, feedback control, and covalent modifications. T/F Examples of Zymogens are the proteases trypsinogen and chymotrypsinogen. T/F? Trypsin catalyzes the removal of dipeptides from inactive chymotrypsinogen and trypsinogen to give the active proteases chymotrypsin and trypsin. T/F The removal of a polypeptide chain from proinsulin produces the active form of insulin. T/F? A kinase can activate an inactive enzyme by phosphorylation, ie adding a phosphate group. T/F? A phosphatase can activate an inactive enzyme by removal of phosphate. T/F? Identify each description of an inhibitor that is either competitive or noncompetitive. A. Increasing substrate reverses inhibition. B. It binds to the enzyme's surface but not to the active site. C. Its structure is similar to that of the substrate.…
Identify the type of enzyme inhibition each of the following inhibitor characteristics is associated with: 1. An inhibitor that decreases enzyme activity by binding to a site on the enzyme other that the active site. 2. An inhibitor that inactivates enzymes by forming a strong covalent bond of the enzyme acitve site.

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