Protein phosphorylation and metabolic control.

E. G. Krebs, J. T. Stull

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

The regulation of enzyme activity through the phosphorylation and dephosphorylation of specific seryl or threonyl residues in enzymes is now recognized as an important control mechanism. A great many non-enzymic proteins may also be interconverted between phosphorylated and non-phosphorylated forms, but in these instances the function served by phosphorylation is not well understood. This lack of understanding is probably due to our lack of knowledge of the specialized actions of most non-enzymic proteins. The sequences of phosphorylation and dephosphorylation of proteins are, of necessity, subject to rigid control. If this were not so, the ATP supply of a cell would be rapidly depleted. Moreover, such processes must be regulated for metabolic interconversions to have a physiological regulatory role. For the best studied system, the interconversion of phosphorylase b and phosphorylase a, many different factors controlling the phosphorylation and dephosphorylation steps have been elucidated. Probably this process is constrained so that it uses only a little energy. In this paper, these constraints are examined.

Original languageEnglish (US)
Pages (from-to)355-367
Number of pages13
JournalCiba Foundation symposium
Issue number31
StatePublished - 1975

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Phosphorylation
Proteins
Phosphorylase b
Phosphorylase a
Enzymes
Adenosine Triphosphate

ASJC Scopus subject areas

  • Medicine(all)

Cite this

Protein phosphorylation and metabolic control. / Krebs, E. G.; Stull, J. T.

In: Ciba Foundation symposium, No. 31, 1975, p. 355-367.

Research output: Contribution to journalArticle

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