Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
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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.
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The mitochondrial form of carbamoyl phosphate synthetase is allosterically activated by N-acetylglutamate. Briefly describe a rationale for this effect.
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.
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
False
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
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- What would be the effect on the activity of phosphofructokinase of the mutation of Asp103 to the unusual amino acid shown below? Explain in terms of actual structures of the side chains of Asp and this unusual amino acid.arrow_forwardThe allosteric properties of aspartate transcarbamoylase have been discussed in detail in this chapter. What is the function of aspartate transcarbamoylase?arrow_forwardWhat would be the metabolic consequences and symptoms of having a mutated form of phosphofructokinase-1 in muscle that is no longer allosterically regulated by [H+]? Speculate on how a patient with this mutation could deal with this.arrow_forward
- Consider a hypothetical enzyme that is COMPLETELY deactivated when a Valine (Val) residue buried in the core of the enzyme is mutated to Glutamate (Glu). In one or two sentences max, explain the MOST LIKELY reason for this occurrence.arrow_forwardExplain the chemical change that occurs in converting kynurenine (a product of tryptophan degradation) to kynurenate, a reaction in which α-ketoglutarate is transformed to glutamate.arrow_forwardExplain why people with a hereditary deficiency of carnitine acyltransferase II have muscle weakness. Why are the symptoms more severe during fasting?arrow_forward
- One metabolic scenario that leads to insulin resistance is the elevation of the conccentration of free fatty acids in skeletal muscle cells. Would you expect increased activity of diacylglycerol acyltransferas (DGAT) to reduce or exacerbate the resistance? Explain.arrow_forwardPhosphonacetyl-L-aspartate (PALA) is a potent inhibitor of aspartate transcarbamoylase because itmimics the two physiological substrates of the enzyme. However, in the presence of substrates, lowconcentrations of PALA increase the reaction rate of aspartate transcarbamoylase. Explain this result.arrow_forwardDicyclohexylcarbodiimide (DCCD) is a reagent that reacts with Asp or Glu residues. Explain why the reaction of DCCD with the c subunits of F1F0-ATP ase blocks its ATP-synthesizing activity.arrow_forward
- Lithium ion inhibits the synthesis of inositol trisphosphate by inhibiting a reaction in the breakdown of inositol trisphosphate.Explain this apparent paradox.arrow_forwardPhosphoglycerate mutase (PGM) catalyzes the interconversion of 3-phosphoglycerate (3PG) and 2-phosphoglycerate (2PG) in the glycolytic and gluconeogenic pathways. a) To what enzyme class does PGM belong? b) There are two distinct classes of PGM, one which is dependent on 2,3-bisphosphoglycerate (2,3-BPG), dPGM, and one which is not, iPGM. dPGM uses acid base chemistry and a phosphorylated histidine residue to interconvert 3PG and 2PG. The dPGM reaction proceeds with formation of 2,3-BPG as an intermediate. Propose a mechanism for the dPGM-catalyzed conversion of 3PG to 2PG that is consistent with this information. c) What is the purpose of 2,3-BPG (i.e., why does dPGM require it)?arrow_forwardAspartate transcarbamoylase, which is necessary for CTP production, is an essential enzyme for the human body. In the below graph, which line represents the rate of the reaction catalyzes by Aspartate transcarbamoylase? Explain.arrow_forward
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