6. An allosteric enzyme has which ofthe following properties?1. It can only operate in an acidicenvironment,2. It can only operate in an alkalineenvironment,3. It becomes active only when itbinds with a specific cofactor,4. It can function either as acatabolic or anabolic enzyme.

Allosteric enzymes are the enzymes that changes their conformation according to the binding of…

Answered: 6. An allosteric enzyme has which of…

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

5. Which class or reactions results in the making of all macromolecules: a) dehydration synthesis of monomersà polymers with the loss of an H2O with the addition of each monomer b) hydrolysis with the addition of one H2O for each reaction c) oxidation with the loss of an e- d) reduction with the gain of an e-
Would you expect the structure of a competitive inhibitor of a given enzyme to be similar to that of its substrate?
1. The enzyme you are studying uses the substrate pictured at right. An inhibitor box in the freezer contains two tubes labeled Inhibitor #1 and Inhibitor #2, along with the structures of the compounds contained within them and their respective Ki. Which one is more likely to be the non-competitive inhibitor? Inhibitor #1 K₁ = 10 μM m CH₂OH OH -0, $ OH OH Inhibitor #2 K₁ = 50 μM Briefly Justify: OH CH₂OH OH OH OH Substrate
Although the first two carbons of fructose and glucose are identical in structure to DHAP and GADP (from glycolysis), DHAP and GADP equilibriate on their in solution to favor the ketone over the aldehyde, while fructose and glucose do not. Why? a)The larger size of the molecule sterically hinders the isomerization b)The larger sugars have more OH groups which hydrogen bond and disrupt isomerization c)The larger sugars cyclize, and there is no carbonyl to isomerize in the cyclic form d)The larger sugars cyclize, and in the cyclic form the hydrogen bonding is very strong e)The larger sugars are less soluble in water than the smaller sugars
4. An enzyme-substrate complex has a Kd = 100 nM. A competitive inhibitor with which of the following Ki values will be most effective at inhibiting this enzyme? A) K₁ = 10 nM B) K₁ = 100 nM C) K₁ = 1000 nM D) None of the above - only the KM is important Briefly explain:
1. Answer the following questions, based on this reaction: S+E P ES EP2 E + P | B)Where is the transition state located?
What kind of catalysis is cysteine driving in this picture? S Los i fy R……—NHR N-H---S O. N-H H-N H-N. O Metal catalysis Covalent catalysis Base catalysis O Acid catalysis NHR²
6. Which class or reactions results in the degradation of all macromolecules: a) dehydration synthesis of monomersà polymers with the loss of an H2O with the addition of each monomer b) hydrolysis with the addition of one H2O for each reaction c) oxidation with the loss of an e- d) reduction with the gain of an e-
Do you think all enzymes would work well at the same pH? why? why would a raddish have a diffrent optimal pH?
4. The enthalpy change of a chemical process depends only on the initial and final conditions, it is independent of the number of intermediate steps in the process. This sums up the ... a) Hess law b) heat additivity law c) law of the enthalpy of formation d) a and b e) a and c f) b and c 5. The reverse activation energy of a certain exothermic reaction is 50 kJ / mol. The direct activation energy of this reaction is: a) greater than 50 kJ / mol b) less than 50 kJ / mol c) 50 kJ / mol d) 0 kJ / mol 6. What is the overall reaction order for the next reaction. 2A + B – 2C + D v = k [A]• [B]* b) 4 c) 3 d) 2 e) 1 5432N1
II. Fill in the blanks with the correct answer. 11. Class of enzyme to which a cis double bond is converted to a trans double bond. 12. Class of enzyme where an alcohol is dehydrated to form a compound with a double bond. 13. Class of enzyme to which an amino group is transferred from one substrate to another. 14. Class of enzyme to which an ester linkage is hydrolyzed. 15. Enzymes that catalyze the following reaction: CH3-Ĉ–COOH → CH3-C-H+ CO2 CH2-0-C-R CH, —ОН CH-0—С—R+ 3H-0 — CH—ОН + 3R-COOH CH2-OH 16. Enzymes that catalyze the following reaction: CH-0-ċ–R ОН 17. Enzymes that catalyze the following reaction: CH3–CH–COOH + NAD* → CH;-C-COOH + NADH + H*

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

6. An allosteric enzyme has which of the following properties? 1. It can only operate in an acidic environment, 2. It can only operate in an alkaline environment, 3. It becomes active only when it binds with a specific cofactor,