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Chapter 18: Problem 15

The sequential action of adenylosuccinate synthetase and adenylosuccinate lyase results in the transfer of an amino group from aspartate and the release of fumarate. Identify two other pairs of enzymes that accomplish the same goal.

Short Answer

Expert verified
Two enzyme pairs that accomplish the same goal as the adenylosuccinate synthetase and lyase are (1) aspartate transaminase and malate dehydrogenase, and (2) alanine transaminase and pyruvate dehydrogenase.

Step by step solution

01

- Understanding Enzyme Action

The enzyme pair in question, adenylosuccinate synthetase and adenylosuccinate lyase, work together in the purine nucleotide cycle to transfer an amino group from aspartate resulting in the release of fumarate. A similar mechanism is seen in various other metabolic pathways where an enzyme pair collaboratively catalyzes the transfer of an amino group from one molecule to another.
02

- Identifying Enzyme Pairs

Let's consider two other enzyme pairs: 1. Aspartate transaminase and Malate Dehydrogenase: This pair of enzymes, acting in sequence, perform the task of transferring an amino group from aspartate to alpha-Ketoglutarate and the subsequent conversion forming Oxaloacetate and Malate respectively while releasing aspartate. 2. Alanine transaminase and Pyruvate dehydrogenase: Another interesting pair of enzymes which resides in Plasmid and mitochondria respectively. Similar to the above pair, these enzyme helps in transferring amino from Alanine to alpha-Ketoglutarate and subsequent conversion to Pyruvate and Acetyl-CoA respectively, with a release of alanine during the process.
03

- Conclusion

In these cases, not only is there the transfer of an amino group from a donor substance to an acceptor, but another product (Fumarate, Oxaloacetate, Pyruvate) is also created.

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Most popular questions from this chapter

The catabolism of fats and carbohydrates provides considerable metabolic energy in the form of ATP. Does the degradation of purines and pyrimidines provide a significant source of energy in eukaryotic cells?

PRPP synthetase uses \(\alpha\)-D-ribose 5 -phosphate as a substrate. How is the \(\alpha\) isomer formed inside the cell?

In eukaryotes, how many ATP equivalents are needed to synthesize one molecule of UMP from \(\mathrm{HCO}_{3}{ }^{\Theta}\), aspartate, glutamine, and ribose 5-phosphate? (Ignore any ATP that might be produced by oxidizing the \(\mathrm{QH}_{2}\) generated in the pathway.)

Identify the nucleotides involved in the following pathways. (a) the nucleotide triphosphate required as a substrate in the synthesis of NAD (b) the nucleotide triphosphate required in the synthesis of FMN (c) the nucleotide triphosphate that serves as a substrate in the synthesis of coenzyme A (d) the substrate for \(\mathrm{G}\) proteins (e) the nucleotide used in the synthesis of glycogen from glucose 6-phosphate (f) the cofactor required in the reaction catalyzed by mammalian succinyl-CoA synthetase (g) the cosubstrate required for the synthesis of phosphatidylserine from phosphatidate (h) the nucleotide required for activation of galactose in cerebroside biosynthesis (i) the nucleotide substrate used in histidine biosynthesis (j) the common precursor of AMP and GMP (k) the precursor of hypoxanthine

Severe combined immunodeficiency syndrome (SCIDS) is characterized by the lack of an immune response to infectious diseases. One form of SCIDS is caused by a deficiency of adenosine deaminase (ADA), an enzyme that catalyzes the deamination of adenosine and deoxyadenosine to produce inosine and deoxyinosine, respectively. The enzyme deficiency increases dATP levels but decreases the levels of other deoxynucleotides, thereby inhibiting DNA replication and cell division in certain rapidly dividing cells. Explain how an adenosine deaminase deficiency affects the levels of deoxynucleotides. (The first effective gene therapy in humans was carried out by transforming a patient's T-cells with a normal ADA gene.)
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