Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
expand_more
expand_more
format_list_bulleted
Question
Chapter 18, Problem 19P
Interpretation Introduction
To justify:
Review the ping-pong mechanism for the uridylyltransferase.
Introduction:
Ping-Pong is the kind of enzyme reaction in which one or more products are released before all substrate binds to the enzyme.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students 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,
#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)
The sedimentation value of aspartate transcarbamoylase decreases when the enzyme switches to the R state. On the basis of the allosteric properties of the enzyme, explain why the sedimentation value decreases.
Chapter 18 Solutions
Biochemistry
Ch. 18 - Characterizing Glycolysis List the reactions of...Ch. 18 - Radiotracer Labeling of Pyruvate from Glucose...Ch. 18 - Effects of Changing Metabolite Concentrations on...Ch. 18 - Prob. 4PCh. 18 - Prob. 5PCh. 18 - The Reactions and Meehanisms of the Leloir Pathway...Ch. 18 - The Effect of lodoacetic Acid on the...Ch. 18 - Prob. 8PCh. 18 - Comparing Glycolysis Entry Points for Sucrose...Ch. 18 - Prob. 10P
Ch. 18 - Prob. 11PCh. 18 - Prob. 12PCh. 18 - Prob. 13PCh. 18 - Energetic of Fructose-1 ,6-bis P Hydrolysis...Ch. 18 - Prob. 15PCh. 18 - Energetics of the Hexokinase Reaction The...Ch. 18 - Prob. 17PCh. 18 - Distinguishing the Mechanisms of Class I and Class...Ch. 18 - Prob. 19PCh. 18 - Understanding the Mechanism of Hemolytic Anemia...Ch. 18 - Prob. 21PCh. 18 - Based on your residing of this chapter, what would...Ch. 18 - Examine the ActiveModel for alcohol dehydrogenase...Ch. 18 - Based on your knowledge of the structure of NAD+...Ch. 18 - Using the ActiveModel for phosphofructokinase...
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_forwardThe Energy Cost of dTTP Synthesis (Integrates with Chapter 20.) Starting from HCO3, glutamine, aspartate, and ribosc-5-P, how many ATP equivalents are consumed in the synthesis of dTTP in a eukaryotic cell, assuming dihydroorotate oxidation is coupled to oxidative phosphorylation? How does this result compare with the ATP costs of purine nucleotide biosynthesis calculated in problem 2?arrow_forwardDe novo purine biosynthesis is a 10-step pathway that builds the purine rings one atom, or one group of atoms, at a time. The pathway converts 5-phosphoribosyl-1-pyrophosphate (PRPP) to inosine monophosphate (IMP). Identify the nine intermediates on the pathway diagram. 5-phosphoribosyl-1-amine PRPP glycinamide ribonucleotide formylglycinamide rimuclocticke N-succinyl-5-aminoimidazole-4- carboxamide ribonucleotide 5-aminoimidazole-4- carboxamide ribonucleotide Incorrect -CH, H H OH Gn Glu -CH. H 0. CH H glycine + ATP HN HC HC ADP+P OH OH OH 0 -PFI HN (P-Ribose Formy-THF HN THE H HN -Ribose -ATP 6-Ⓡ CH₂ HN HC CH, P-Ribose -ATP ADP+P NH, ADP+P HN NH -Ribose NH, N-formylaminoimidazole-4- carboxamide ribonucleotide formylglycinamidine ribonuclcotide S-aminoimidazole ribonuclotidie ATP ADP+Pi HCO, carboxyanincimidazole ribonucleotide -Ribose H -Ribose H₂O Formyl-THF- ASP Fumarate HC THE 0 N. "NH₂ Ⓒ-Abse NH, NH, -ATP NH -N-CH COO ADP+PI Coo IMP COO NH, 000 Answer Bankarrow_forward
- The mitochondrial form of carbamoyl phosphate synthetase is allosterically activated by N-acetylglutamate. Briefly describe a rationale for this effect.arrow_forwardStructural similarity between the SARS-CoV-2 Mpro protease and chymotrypsin suggests that they would use the same catalytic mechanisms. What feature of the active site would you expect to find in Mpro that would be important in stabilizing the transition state? Describe how that feature would act to stabilize the transition state.arrow_forwardIntramitochondrial ATP concentrations are about 5 mM, and phosphate concentration is about 10 mM. If ADP is five times more abundant than AMP, calculate the molar concentrations of ADP and AMP at an energy charge of 0.85. Calculate AG for ATP hydrolysis at 37 °C under these condi- tions. The energy charge is the concentration of ATP plus half the concen- tration of ADP divided by the total adenine nucleotide concentration: [ATP] + 1/2[ADP] [ATP] + [ADP] + [AMP]arrow_forward
- Why the catalytic residue mutants of Glycoside hydrolase still remain a lot activity ?arrow_forwardGlutamine affects the regulatory system for E. coli glutamine synthetase so as to promote the adenylylation of glutamine synthetase and inhibit the deadenylylation. Why do these effects make good metabolic sense?arrow_forwardPhosphoribosyltransferase (PRT) catalyzes the attachment of a salvaged purine nitrogenous base on the activated form of ribose-5-phosphate called 5-phosphoribosyl- α α-pyrophosphate ( α α-PRPP). True Or Falsearrow_forward
- Amino transferases catalyze the transfer of amino groups to alpha-keto acids with pyridoxal phosphate as the prosthetic group. Pyridoxal phosphate can accept an amino group, and its aminated form, pyridoxamine phosphate, can donate its amino group to an alpha-keto acid. Illustrate the detailed mechanism of the transamination reaction in the active site of an aminotransferase. Use the glutamate oxaloacetate transaminase as an example.arrow_forwardThe reaction catalyzed by phosphorylase is readily reversible in vitro. At pH 6.8, the equilibrium ratio of orthophosphate to glucose 1-phosphate is 3.6. The value of ΔG°’ for this reaction is small because a glycosidic bond is replaced by a phosphoryl ester bond that has a nearly equal transfer potential. However, phosphorolysis proceeds far in the direction of glycogen breakdown in vivo. Suggest one means by which the reaction can be made irreversible in vivo.arrow_forwardRefer to the reaction scheme of the GAPDH catalyzed formation of 1,3-BPG. In the reaction, the nucleophile in step (4) is an inorganic phosphate molecule. The enzyme active site is elaborately constructed so that inorganic phosphate, not water, acts as the nucleophile. What advantage is gained by using inorganic phosphate, instead of water, as the nucleophile? Discuss in terms of the energy yield of glycolysis. No need to calculate the total net energy yield of glycolysis.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