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
Question
Chapter 26, Problem 10P
Interpretation Introduction
Interpretation:
A balanced equation for the conversion of asparate to fumarate by the purine nucleoside cycle in skeletal muscle.
Concept introduction:
The conversion of IMP to AMP may be a transamination reaction during which IMP is a keto acceptor.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
Intramitochondrial 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]
The protein fragments ABS1 and ABS2 of tropomodulin were produced as fusion proteins with chitin binding domain and purified by a chitin column. Explain the principles of this type of affinity chromatography and support it with a self‐drawn figure. This is with regards to Tropomodulin/ F-Actin complex.
The allosteric properties of aspartate transcarbamoylase have been discussed in detail in this chapter. What is the function of aspartate transcarbamoylase?
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
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
- Refer 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_forwardExplain how the pKa for histidine 57 is important to its role in the mechanism of chymotrypsin actionarrow_forwardFructose 1,6-bisphosphatase (FBPase) is a key enzyme in gluconeogenesis. The mammalian enzyme is tetrameric, negatively regulated by both Fructose 2,6-bisphosphate and AMP. Propose three (3) distinct models for how these molecules regulate FBPase activity. Also, describe how the enzyme might differentiate between Fructose 1,6 bisphosphate and Fructose 2,6-bisphosphate binding to the allosteric site on the enzyme with particular emphasis on amino acids comprising the allosteric binding site(s).arrow_forward
- When hyaluronan synthase from Pasteurella multocida was expressed in E. coli, the bacteria spun out a capsule of hyaluronan. This reaction was analyzed using purified membrane fragments containing the hyaluronan synthase, a radio-labeled tetrasaccharide acceptor (Part A), along with the activated forms of the sugar subunits: UDP-N-acetylglucosamine and UDP-glucuronic acid. In short incubations with the complete mixture, the tetrasaccharide primer elongated by several units, although only odd-numbered chains were visible (Part B lane 2). If one or both activated sugars were left out, the results shown in lanes 3-5 (Part B) were obtained. Why do you suppose that only odd-number chains are visible in your assay? (A) ACCEPTOR nonreducing end HO- HO OH COO glucuronic acid (GICUA) HO- CH3 T C=O I NH CH₂ OH N-acetylglucosamine (GlcNAc) COO но- HO OH OH I CH₂ reducing end NH C=O CH3 Choose one: O A. Synthase adds GlcNAc much more slowly than it adds GICUA. O B. One of the monosaccharide…arrow_forwardResidue Asn 204 in the glucose binding site of hexokinase IV was mutated, in two separate experiments, to either Ala or Asp. The Asn → Ala mutant had a KM nearly 50-fold greater than the wild-type enzyme, and the Asn → Asp mutant had a 140-fold greater KM value than the wild-type enzyme. These mutations impact the intermolecular interactions between the enzyme and the glucose substrate.The amide functional group of the Asn side chain can form with the hydroxyl groups of the glucose substrate and can potentially function as either a . The methyl group of Ala cannot participate in hydrogen bond formation, which explains the in glucose affinity as indicated by the higher KM for the mutant enzyme. The side chain of Asp could potentially serve as a , but…arrow_forwardResidue Asn 204 in the glucose binding site of hexokinase IV was mutated, in two separate experiments, to either Ala or Asp. The Asn → Ala mutant had a KM nearly 50-fold greater than the wild-type enzyme, and the Asn → Asp mutant had a 140-fold greater KM value than the wild-type enzyme. These mutations impact the intermolecular interactions between the enzyme and the glucose substrate.The amide functional group of the Asn side chain can form (dipole-dipole interactions, hydrodgen bonds, London Dispersion Interactions, or Ion-Dipole Interactions) with the hydroxyl groups of the glucose substrate and can potentially function as either a (hydrogen bond donor and/or acceptor, hydrogen bond donor, or hydrogen bond acceptor) . The methyl group of Ala cannot participate in hydrogen bond formation, which explains the (increase or decrease)…arrow_forward
- Phosphoribosyltransferase (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_forwardWill the amount of glycogen be higher or lower than normal or unchanged? Pyridoxal phosphate is covalently bonded to glycogen phosphorylase via a Schiff base to Lys 680. What effect would the mutation of Lys680Ala have on the breakdown of glycogen?(This notation means the following: K680 is the normal amino acid in this enzyme. It has been mutated to 680A.) Loss of the gene for the kinase that phosphorylates GSK3 on glycogen synthesis. Effect of the substrate analog below on glycogen synthesis.arrow_forwardWrite a balanced equation for the synthesis of TMP from dUMP that is coupled to the conversion of serine into glycine.arrow_forward
- Why Phenylmethylsulfonyl fluoride (PMSF, shown in Fig.) does not inhibit aspartate protease as potent as serine protease?arrow_forwardThe enzyme aspartate transcarbamoylase catalyzes an early step in pyrimidine biosynthesis. The two states of the multi-subunit enzyme are shown below. Note that the binding of the regulatory molecule CTP (cytosine triphosphate) causes the enzyme complex to be inactive. Is this situation an example of positive or negative regulation? Explain why the use of CTP as the regulatory molecule is logical givén the overall function of this particular enzyme. INACTIVE ENZYME: T STATE catalytic subunits regulatory subunits OFF 6 CTP ON ACTIVE ENZYME: R STATEarrow_forwardConsidering the gluconeogenesis that may occur after removal of the amino group from amino acids, will malate be an intermediate in all such metabolic routes between amino acids and glucose? Explain. The phosphoenolpyruvate carboxykinase (PEPCK) gene is more actively transcribed when glucagon is present in blood. Putting the signal cascade responsible for that activation aside for the moment, will the reaction that PEPCK mediates be in zero or first order for that increased transcription to have a maximal affect on gluconeogenesis? Explain.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
Macromolecules | Classes and Functions; Author: 2 Minute Classroom;https://www.youtube.com/watch?v=V5hhrDFo8Vk;License: Standard youtube license