Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
expand_more
expand_more
format_list_bulleted
Concept explainers
Question
Chapter 31, Problem 15P
Interpretation Introduction
Interpretation :
The indicated mechanism needs to be explained.
Interpretation :
HtrA proteins and their orthologues signify the vital class of the heat-shock-induced serine proteases plus chaperones shielding the structure of protein. They are stated in both eukaryotic and prokaryotic species, comprising humans and plants.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
Need help
Sesamin is one of the major lignans found in sesame oil. Sesamin-metabolic pathways remain uncharacterized at both the enzyme and gene levels. However, one microorganism showed significant sesamin-degrading activity and was identified as Sinomonas sp. no. 22. A sesamin- metabolizing enzyme named SesA was purified from this strain and characterized. Explain how sesamin methylene transferase was identified and characterized and explain the mechanism. Based on your knowledge, what other assays could be run to characterize this enzyme?
M-CSA Mechanism and Catalytic Site Atlas (ebi.ac.uk)
(ii)
Acyl Carrier Protein S-acetyltransferase (EC 2.3.1.38) is a transferase enzyme that
catalyzes the first biosynthetic pathway for fatty acid synthase. It transfers the acyl
group (CH3CO) first from coenzyme A to a cysteine residue in the active site. This is
similar to what happens in Chymotrypsin, however utilizing a sulfur instead of an
oxygen. The acyl group is then transferred to the molecule ACP. Provide the enzyme-
catalyzed mechanism for the reaction below, making sure to identify the roles of all key
amino acids:
i
H3C
SCOA
acetyl COA
enzyme
+ HS
i
H3C
SACP
acetyl ACP
Predict the effect of each of the following amino acid substitutions on the KM and kcat of the enzyme-catalyzed reactions
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
- Approximately how much does staphylococcal nuclease (Table) decrease the activation free energy ΔG‡ of its reaction (the hydrolysis of a phosphodiester bond) at 25°C?arrow_forwardA synthetic substrate, the para-nitrophenylacetate (PNPA), is used to monitor enzyme activity of protein P. The product of the hydrolysis reaction absorbs at 410 nm with a molar extinction coefficient of 4 000 M-¹.cm-¹. 1- Write the reaction catalyzed by the protease P using the pNPA substrate. 2- The enzyme extract is too concentrated and a 1/300 dilution is needed for enzyme tests. Considering that you would need at least 600 µL of diluted enzyme extract for activity tests, indicate which volume of buffer and enzyme extract you must use for the dilution.arrow_forwardNeed help with this problem!arrow_forward
- d. Which of the substrates is likely to have a higher Vmax. What is your reasoning? e. Can you propose a molecule that might act as an inhibitor to this reaction? Explain your reasoning.arrow_forwardMany enzyme -catalyzed reactions are consistent with a modified version of the Michaelis -Menten mechanism in which the second step is also reversible. For this mechanism obtain an expression for the rate of formation of product and find its limiting behavior for large and small concentrations of substrate using steady state approximationarrow_forwardNeed help, please.arrow_forward
- Make an electron-flow-mechanism for this synthetic scheme. This involves predicting major and by-products using electronic and structural effects. The arrow push mechanism must be shown.(from the reaction of α-ketoacids and oxaprolines to proteins that contain native serine residues ) with labelarrow_forwardUsing the ActiveModel for aldose reductase, describe the structure of the TIM barrel motif and the structure and location of the active site.arrow_forwardDistinguishing the Mechanisms of Class I and Class I Aldolases Fructose bisphosphate aldolase in animal muscle is a class 1 aldolase, which forms a Schiff base intermediate between substrate (for example. fructose-1, 6-bisphosphate or dihydroxyacetone phosphate) and a lysine at the active site (see Figure I8.12). The chemical evidence for this intermediate conies from studies with aldolase and the reducing agent sodium borohydride, NaBH4. Incubation of the enzyme with dihydroxyacetone phosphate and NaBH4 inactivates the enzyme. Interestingly, no inactivation is observed if NabH4 is added to the enzyme in the absence of substrate. Write a mechanism that explains these observations and provides evidence for the formation of a Schiff base intermediate in the aldolase reaction.arrow_forward
- 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.arrow_forward7.arrow_forward1. pH Effects a. In the enzyme mechanism of lysozyme, two acidic amino acid residues, Asp52 and Glu35, are critical for catalytic activity. If we assume normal side chain pKa values for Asp (pKar = 3.90) and for Glu (pKar = 4.07), what proportion of enzyme molecules will have both Asp52 and Glu35 in the correct ionization state at pH 5.0 (the pH optimum for lysozyme)? b. Are the traditional pKa values likely to be correct within the protein? What pKa changes might be present within lysozyme?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
Macromolecules | Classes and Functions; Author: 2 Minute Classroom;https://www.youtube.com/watch?v=V5hhrDFo8Vk;License: Standard youtube license