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Regulation of Protein Biosynthesis

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Principles of Metabolic Control in Mammalian Systems

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Abstract

Before embarking on a consideration of the regulation of protein bio-synthesis, it may be useful to examine the need for protein biosynthesis. Although the life process depends absolutely on structural and functional proteins, it seems reasonable to inquire why, once proteins and enzymes are synthesized, the system does not remain stable, requiring no further protein synthesis. The answer has been dealt with in Chapters 1, 2, and 3. Suffice it to say here that enzymes function by virtue of their conformability, using noncovalent forces that permit substrate binding and product release in addition to the catalytic action of making and breaking covalent bonds in the substrate. The details of this process are treated in Chapter 3. Because of this conformability, which depends on noncovalent forces, enzymes are subject to denaturation and consequent loss of function; hence, enzymes are semistable. The relatively delicate balance between form, functionality, and denaturation is maintained, on one hand, by the orderly process of enzyme biosynthesis, and, on the other, by degradation of denatured enzymes.

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Authors and Affiliations

  1. Department of Metabolic Research, Children’s Hospital of Philadelphia, University of Pennsylvania, Philadelphia, Pennsylvania, 19104, USA

    Robert M. Cohn & Pamela D. McNamara

  2. Endocrine-Metabolic Service, Letterman Army Medical Center, Presidio of San Francisco, California, 94129, USA

    Robert H. Herman

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  1. Robert M. Cohn
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  1. Letterman Army Institute of Research, San Francisco, California, USA

    Robert H. Herman

  2. University of Pennsylvania, Philadelphia, Pennsylvania, USA

    Robert M. Cohn  & Pamela D. McNamara  & 

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Cohn, R.M., McNamara, P.D., Herman, R.H. (1980). Regulation of Protein Biosynthesis. In: Herman, R.H., Cohn, R.M., McNamara, P.D. (eds) Principles of Metabolic Control in Mammalian Systems. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-3006-6_5

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