enzyme active siteSer-CH₂-C195Asp102substrate15. A substrate binds to enzyme active site.a) List the roles of serine, histidine and aspartic acidb) Show how the first tetrahedral intermediate would be formed.c) Show acyl-enzyme intermediate.d) What is the pka for Histidine? How is this pka relate to physiological pH(7.4)? Do you anticipate any enzymatic reaction will occur if histidine isreplaced with cysteine? Why?

The enzyme has serine, histidine and aspartate in the active site. Serine proteases are protein…

Answered: 15. A substrate binds to enzyme active…

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

Legend: Blue – wild-type β-galactosidase Red – mutant β-galactosidase _________ a. What is the optimum pH of wild type β-galactosidase? _________ b. What is the optimum temperature of mutant β-galactosidase? _________ c. Which enzyme has the greater activity at pH 7.2? _________ d. Which enzyme has the greater activity at a temperature of 42.5oC? _________ e. Which enzyme has greater activity if pH decreases from 7.5 to 6.4? _________ f. Which enzyme has greater activity if temperature increases from 40oC to 41 oC?
Enzyme Combination - Cla I + EcoRI What is the number of fragments? What are/is the size(s) of fragment(s)?
Note:- Provide detailed explanation for the reaction that involves the removal of nitrogen from an alpha-amino acid, forming an alpha-keto acid. Please explain with the help of an example.
1. Depict the structure features in the active site of cysteine protease 2. provide a step-wise reaction mechanism to show the hydrolysis of the peptide bond catalyzed by a cysteine protease
19. Define the terms “cofactor” and “coenzyme.” 20. What is the difference between general acid-base catalysis and specific acid-base catalysis? (Assume that the solvent is water.)
Under certain conditions, peptide bond formation rather than peptide bond hydrolysis is thermodynamically favorable. Would you expect chymotrypsin to catalyze peptide bond formation? Explain.
Describe the nitrogenase complex. How is the enzymeorganized? What are its unique components?
#1 Specify the role each of the following amino acids play within the crystal structure and/or active site for Be as specific as possible, with pictures (and mechanistic arrows) as necessary. His11 Arg140 Glu89 Trp68 #2 Provide a step-wise mechanism for the reaction Bisphosphoglycerate mutase catalyzes, using the amino acids responsible for aiding in catalysis. You do not need to add surrounding amino acids that aid in substrate specificity. (drawn out)
if the reaction pH drops significantly (pH=2 for example), how would reaction catalyzed be serine proteases be affected? why? (assumin that the rest of the protein structure remain intact)
How would chymotrypsin's catalytic triad be affected by extremely low and extremely high pH values (assuming the rest of the protein remains intact)?
Proteins treated with proteolytic enzymes hydrolyzed peptide bonds to yield a mixture of amino acids only. Is the statement TRUE OR FALSE?
6 The following structure is part of the lipopolysaccharide found on the outside of vibrio cholerae. I know that the glycosidic linkage connecting residues B and C and the glycosidic linkage connecting residues C and D are both alpha, but what are the numbers that follow the alpha? Ex: alpha- ? -> ?

SEE MORE QUESTIONS

Recommended textbooks for you

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Biology: The Dynamic Science (MindTap Course List)

Biology

ISBN:

9781305389892

Author:

Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:

Cengage Learning

Biology 2e

Biology

ISBN:

9781947172517

Author:

Matthew Douglas, Jung Choi, Mary Ann Clark

Publisher:

OpenStax

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Biology: The Dynamic Science (MindTap Course List)

Biology

ISBN:

9781305389892

Author:

Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:

Cengage Learning

Biology 2e

Biology

ISBN:

9781947172517

Author:

Matthew Douglas, Jung Choi, Mary Ann Clark

Publisher:

OpenStax

SEE MORE TEXTBOOKS