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Berg JM, Tymoczko JL, Stryer L. Biochemistry. 5th edition. New York: W H Freeman; 2002.

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Biochemistry. 5th edition.

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Chapter 23Protein Turnover and Amino Acid Catabolism

Degradation of cyclin B.

Figure

Degradation of cyclin B. This important protein in cell cycle regulation is visible as the green areas in the images above (the protein was fused with green fluorescent protein). Cyclin B is prominent during metaphase, but is degraded in anaphase to prevent (more...)

The assembly of new proteins requires a source of amino acids. These building blocks are generated by the digestion of proteins in the intestine and the degradation of proteins within the cell. Many cellular proteins are constantly degraded and resynthesized. To facilitate this recycling, a complex system for the controlled turnover of proteins has evolved. Damaged or unneeded proteins are marked for destruction by the covalent attachment of chains of a small protein, ubiquitin. Polyubiquitinated proteins are subsequently degraded by a large, ATP-dependent complex called the proteasome.

The primary uses of amino acids are as building blocks for protein and peptide synthesis and as a source of nitrogen for the synthesis of other amino acids and other nitrogenous compounds such as nucleotide bases. Amino acids in excess of those needed for biosynthesis cannot be stored, in contrast with fatty acids and glucose, nor are they excreted. Rather, surplus amino acids are used as metabolic fuel. The α-amino group is removed, and the resulting carbon skeleton is converted into a major metabolic intermediate. Most of the amino groups of surplus amino acids are converted into urea through the urea cycle, whereas their carbon skeletons are transformed into acetyl CoA, acetoacetyl CoA, pyruvate, or one of the intermediates of the citric acid cycle. Hence, fatty acids, ketone bodies, and glucose can be formed from amino acids.

Several coenzymes play key roles in amino acid degradation, foremost among them is pyridoxal phosphate. This coenzyme forms Schiff-base intermediates that allow α-amino groups to be shuttled between amino acids and ketoacids. We will consider several genetic errors of amino acid degradation that lead to brain damage and mental retardation unless remedial action is initiated soon after birth. Phenylketonuria, which is caused by a block in the conversion of phenylalanine into tyrosine, is readily diagnosed and can be treated by removing phenylalanine from the diet. The study of amino acid metabolism is especially rewarding because it is rich in connections between basic biochemistry and clinical medicine.

  • 23.1. Proteins Are Degraded to Amino Acids
  • 23.2. Protein Turnover Is Tightly Regulated
  • 23.3. The First Step in Amino Acid Degradation Is the Removal of Nitrogen
  • 23.4. Ammonium Ion Is Converted Into Urea in Most Terrestrial Vertebrates
  • 23.5. Carbon Atoms of Degraded Amino Acids Emerge as Major Metabolic Intermediates
  • 23.6. Inborn Errors of Metabolism Can Disrupt Amino Acid Degradation
  • Summary
  • Problems
  • Selected Readings

By agreement with the publisher, this book is accessible by the search feature, but cannot be browsed.

Copyright © 2002, W. H. Freeman and Company.
Bookshelf ID: NBK21182

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