Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
expand_more
expand_more
format_list_bulleted
Question
Chapter 26, Problem 18P
Interpretation Introduction
Interpretation:
The structure corresponding to the MWC R-state and T-state needs to be determined.
Concept introduction:
Beta sheet structure or five −sheet strand is comprises of two parallel strand and one anti-parallel strand and these two strands are joined by the other two parallel strands and this sheet structure is used as the CTP binding site. A sheet can also be represent in the other form which consists of four stranded sheet and two − alpha helices. Therefore, structure consists three layers which are sheet, helix and sheet.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
Consider the role of Histidine in the Serine protease mechanism and sketch a plot showing
the predicted pH profile of chymotrypsin which has a pH optimum of approximately ~8. The pk,
for the His in the catalytic triad is 7.3 in free chymotrypsin which increases to greater than 8 with
a bound peptide. Be sure to label the plot axes and indicate the pka of His on the plot,
Chart is Given for you: Below is a chart of values for actual enzymes.
Enzyme Km (M) kcat (1/s)Chymotrypsin 1.5 × 10^−2 0.14Pepsin 3.0 × 10^−4 0.5Tyrosyl-tRNA synthetase 9.0 × 10^−4 7.6Ribonuclease 7.9 × 10^−3 7.9 × 10^2Carbonic anhydrase 2.6 × 10^−2 4.0 × 10^5Fumarase 5.0 × 10^−6 8.0 × 10^2
Assume the enzyme concentration is equal across all samples (and is equal to 1).
(Answer a and b only)a. Which enzyme will have the highest V0 at very high substrate concentrations? (1 M). Why?
b. Which will have the highest V0 at very low substrate concentrations (5.0 × 10^−12). Why?
. The optimal conditions for salivary lysozyme (hydrolyzing glycoproteins of bacterial
wall) are 37 C - temperature and pH is 5.2. Explain the decrease in this enzyme
activity if the temperature will rise up to 60 °C and pH will be changed to 8.0. To
answer the question:
a) draw the graph of the velocity dependency on temperature and pH;
b) calculate the relative enzyme activity if 10 mg of lysozyme catalyzes the
formation of 5 uM of the product per 2 minutes.
Concidor
NH3:
5.
Chapter 26 Solutions
Biochemistry
Ch. 26 - Prob. 1PCh. 26 - Prob. 2PCh. 26 - Allosteric Regulation of Purine and Pyrimidine...Ch. 26 - Inhibition of Purine and Pyrimidine Metabolism by...Ch. 26 - Prob. 5PCh. 26 - Allosteric Regulation of Ribonucleotide Reductase...Ch. 26 - Prob. 7PCh. 26 - Prob. 8PCh. 26 - Prob. 9PCh. 26 - Prob. 10P
Knowledge Booster
Similar questions
- Using the ActiveModel for aldose reductase, describe the structure of the TIM barrel motif and the structure and location of the active site.arrow_forwardCan you please describe the specific components that each of these structures are comprised of ( alpha helices and beta sheets) in more detail? Also, what do the different colors represent? Your reply will be greatly appreciated. The ligand that was assigned to me is tadalafil.arrow_forwardShown below is a substrate for a Trypsin. Draw the mechanism for this serine protease using the artificial substrate. Be sure to draw the catalytic triad, and show the role of the oxyanion hole. Draw the complete structure of every intermediate and product and PUSH ARROWS!!!!! Do not abbreviate structures using R and R' H₂N _N_CH. сно CH₂ CH₂ CH₂ NH d=19H₂ NH₂ O CH- H₂C HN O CHarrow_forward
- 5) Consider the hypothetical biochemical pathway shown below. Assume that each letter (A, B, C, etc) represents a molecule and each number over an arrow (1, 2, 3, etc) represents an enzyme that catalyzes that reaction (so enzyme 2 catalyzes the conversion of B to C). Indicate all the probable feedback inhibition interactions that would be expected to regulate the activity of enzymes in this pathway. please indicate each interaction in the format example: "X will inhibit enzyme 27".arrow_forwardprotease mechanism: you isolate a new protease which cleaves the peptide bond 2 aa residues before a F residue. You might expect to fınd... O An I residue in the S2'pocket AL residue in the S2 pocket O aV residue in the oxyanion hole An Lresidue in the catalytic triad in Michaelis-Menton kinetics, cutting the enzyme concentration in half will O will double the reaction rate O will not change Vo and Vmax will change Vo but not turnover number decrease Km by halfarrow_forward1967, Rabin demonstrated that a single substrate reaction catalised by an enzyme that has a single binding site for the substrate, can show sigmoidal kinetics. Discuss this scenario so that it is clear why a plot of Vo versus [SJ at fixed total enzyme concentration will be sigmoidal.arrow_forward
- Prepare a schematic diagram and present it as though it were a Figure in a publication (scientific journal or textbook) The diagram should illustrate the interactions made between the key components of (a) total and (b) non-specific binding reactions. In preparing your diagram,you should reflect on the role of each of the components of the reaction mixtures, and why the subtraction of non-specific from total binding allows us to calculate specific binding. The diagram Legend should be brief but informative.arrow_forward>1HPL_1|Chains A, B|LIPASE|Equus caballus (9796) NEVCYERLGCFSDDSPWAGIVERPLKILPWSPEKVNTRFLLYTNENPDNFQEIVADPSTIQSSNFNTGRKTRFIIHGFIDKGEESWLSTMCQNMFKVESVNCICVDWKSGSRTAYSQASQNVRIVGAEVAYLVGVLQSSFDYSPSNVHIIGHSLGSHAAGEAGRRTNGAVGRITGLDPAEPCFQGTPELVRLDPSDAQFVDVIHTDIAPFIPNLGFGMSQTAGHLDFFPNGGKEMPGCQKNVLSQIVDIDGIWQGTRDFAACNHLRSYKYYTDSILNPDGFAGFSCASYSDFTANKCFPCSSEGCPQMGHYADRFPGRTKGVGQLFYLNTGDASNFARWRYRVDVTLSGKKVTGHVLVSLFGNKGNSRQYEIFQGTLKPDNTYSNEFDSDVEVGDLEKVKFIWYNNVINLTLPKVGASKITVERNDGSVFNFCSEETVREDVLLTLTAC Can you find the biological Function of horse pancreatic acid and highlight the catalytic amino acids in a row and active sites from the above sequence of 1HPLarrow_forwardRuBP carboxylaseis by no means an idesl enzyme. Describe some of the problems with its active site and its substrate specificity. If we compare the amino acid sequences of this enzyme from many different species, they are almost identical. What is the significance of this uniformity?arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
- BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage LearningBiology: The Dynamic Science (MindTap Course List)BiologyISBN:9781305389892Author:Peter J. Russell, Paul E. Hertz, Beverly McMillanPublisher:Cengage Learning
Biochemistry
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