Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
expand_more
expand_more
format_list_bulleted
Concept explainers
Videos
Textbook Question
Chapter 19, Problem 3P
Assessing the Effect of Active-Site Phosphorylation on Enzyme Activity (Integrates with Chapter 15.) The serine residue of isocitrate dehydroenase that is phosphorylated by protein kinase lies within the active site of the enzyme. This situation contrasts with most other examples of coa1ent modification by protein phosphorylation. where the phosphorylation occurs at a sate remote from the active site. What direct effect do you think such active-site phosphorylation might have on the catalytic activity of isocitrate dehydrogcn.ise? (Sec Barford, D., 1991. Molecular mechanisms for the control of enzymic activity by protein phosphorytation. Biochimica et Biophysica Acta 1133:55—62.)
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
Fozyme Action: An Investigation of Lactase Activity
137
PART F EFFECT OF pH ON ENZYME ACTIVITY
Activity of Lactaid at Several pls
Observation with Tes Tape"
Glucose present?
Lactose
90 change
More Grean tello
Green Hellow
NO change
Green
NO
pH 7
Yes, 100 mgloL
pH 2
Yes
7100 mglaL
pH 10
NO
Glucose
tes 300 mglaL
RART G. EFFECT OF AN INHIBITOR ON ENZYME ACTIVITY
Inhibitor Effects
Observation with Tes Tape
Glucose present?
Light Green
Teal
Yellow IGreen
Dark Brown
Lactose
Yes
Lactaid"
NO
Ethanol
Yes
Yes
Glucose
1. What is the optimum pH of the lactose-conversion reaction, as shown by your data?
2 Did ethanol act as an efficient inhibitor of the lactose conversion to glucose and galactose?
3. Summarize your findings about the concentration, temperature, and pH sensititivity of lactase.
whether a protein can to work in the same way in two different types of cells
and if it possible that the same protein might function in different biochemical pathways
in eye cells and muscle cells even if the protein's basic mechanism always remains the same.
MA
Inducers and Inhibitors of AEP.
Short peptides such as legumain stabilization and activity modulation (LSAM) domain and αvβ3 integrin could enhance the activity of AEP. LSAM domain known as the prodomain of AEP blocks substrate binding before activation. This prodomain has a helical structure and two independent peptides. One is an activation peptide (AP, K287 to N323), and the other is a LSAM domain. LSAM domain remains even after AP is cleaved and released from protease at neutral pH via electrostatic interaction. AEP without LSAM domain has a lower melting temperature than AEP with LSAM domain [77, 117]. Another short peptide, αvβ3 integrin, can directly interact with AEP, and after forming a complex, the optimal pH for AEP activity is increased from 5.5 to 6.0. It indicates that αvβ3 binding could induce conformational stabilization of AEP accompanied by deprotonated C189. αvβ3 does not directly interact with the AEP active site; however, AEP docks to the αvβ3 RGD-binding site…
Chapter 19 Solutions
Biochemistry
Ch. 19 - Radiolabeling with 14C-Glutamate Describe the...Ch. 19 - Prob. 2PCh. 19 - Assessing the Effect of Active-Site...Ch. 19 - Understanding the Mechanism of the -Ketoglutarate...Ch. 19 - Understanding the Action of Fluoroacetate on the...Ch. 19 - Prob. 6PCh. 19 - Prob. 7PCh. 19 - Prob. 8PCh. 19 - Prob. 9PCh. 19 - Prob. 10P
Ch. 19 - Prob. 11PCh. 19 - Prob. 12PCh. 19 - Prob. 13PCh. 19 - Prob. 14PCh. 19 - Prob. 15PCh. 19 - Prob. 16PCh. 19 - Understanding the Oxidation of Glucose and Its...Ch. 19 - Prob. 18PCh. 19 - Prob. 19PCh. 19 - Prob. 20PCh. 19 - Complete oxidation of a 16-carbon fatty acid can...Ch. 19 - Study Figure 19.18 and decide which of the...Ch. 19 - Prob. 23P
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.Similar questions
- Regulation of Glutamine Synthetase by Covalent Modification Suppose at certain specific metabolite concentrations in vivo the cyclic cascade regulating E. coli glutamine synthetase has reached a dynamic equilibrium where the average state of GS adenylylation is poised atn=6. Predict what change in nwill occur if: [ ATP ] increases, PIIA/PIID increases, [ -KG ]/[ Gln ] increases, [ Pi ] decreases.arrow_forwardbiosynthesis of Thymidine monophosphate from ATP, HCO3-, Gln, Asp, quinone, and methylene THF. Show your work and don’t forget that the conversion of U to T only happens AFTER Ribonucleotide Reductase processes the 2’, 3’ ribose to the 3’ deoxy ribosearrow_forwardKetosis in Dairy Cattle: 1. Explain why propionate can contribute to the next synthesis of glucose but acetic acid cant.arrow_forward
- Kk155.arrow_forwardLocalization of Molecules and Functions Within the Mitochondrion. Indicate whether you would expect to find each of the following molecules or functions in the matrix (MA), the inner membrane (IM), the outer membrane (OM), the intermembrane space (IS), or not in the mitochondrion at all (NO). Write abbreviation in front of the molecules. No explanation is required. Succinate dehydrogenase Coenzyme A Conversion of lactate into pyruvate ATP synthase Malate dehydrogenase Pyruvate Citrate synthase Cristae Accumulation of a high proton concentration Pyruvate dehydrogenasearrow_forwardOnly typed explanation which statements are true?arrow_forward
- Comparing the active site geometries of chymotrypsin and subtilisin enzymes under the hypothesis that their similarities had catalytic importance led to a greater mechanistic knowledge of both enzymes (which they did not). Can you discuss the efficacy of this tactic?arrow_forwardgeneration of one less FADH2 molecule. Part C B-oxidation dealls with only saturated fatty acids, but many fatty acids in natural lipids are unsaturated, meaning they contain one or more double bonds. Considering the fatty acid below, calculate the energy yield of its complete oxidation. OH Express your answer using three significant figures. ▸ View Available Hint(s) ΑΣΦ + 0 ? Submit ATParrow_forwardPlease check my work and make corrections for parts A, B, and C and explain the answer for part D. Thank you!arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning
Anaerobic Respiration; Author: Bozeman Science;https://www.youtube.com/watch?v=cDC29iBxb3w;License: Standard YouTube License, CC-BY