Trends Biochem Sci. 1992 Mar;17(3):114-9.

Dual-specificity protein kinases: will any hydroxyl do?

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Molecular Biology and Virology Laboratory, Salk Institute for Biological Studies, San Diego, CA 92186-5800.

Abstract

Protein kinases are classified by the target amino acid in their substrates. Those protein kinases that phosphorylate hydroxyamino acids comprise two groups, the protein-tyrosine and protein-serine/threonine kinases, which, until recently, had been thought to be mutually exclusive. However, several new protein kinases have been discovered that, by the criterion of primary structure, would be classified as protein-serine/threonine kinases but which, surprisingly, are able to phosphorylate tyrosine residues. Even more surprising, there are reports of protein kinases that are capable of phosphorylating both tyrosine and serine/threonine residues. We review and discuss recent developments concerning these 'dal-specificity' protein kinases.

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Dual-specificity protein kinases: will any hydroxyl do?
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