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  • Title: A mutation in the catalytic subunit of cAMP-dependent protein kinase that disrupts regulation.
    Author: Levin LR, Kuret J, Johnson KE, Powers S, Cameron S, Michaeli T, Wigler M, Zoller MJ.
    Journal: Science; 1988 Apr 01; 240(4848):68-70. PubMed ID: 2832943.
    Abstract:
    A mutant catalytic subunit of adenosine 3',5'-monophosphate (cAMP)-dependent protein kinase has been isolated from Saccharomyces cerevisiae that is no longer subject to regulation yet retains its catalytic activity. Biochemical analysis of the mutant subunit indicates a 100-fold decreased affinity for the regulatory subunit. The mutant catalytic subunit exhibits approximately a threefold increase in Michaelis constant for adenosine triphosphate and peptide cosubstrates, and is essentially unchanged in its catalytic rate. The nucleotide sequence of the mutant gene contains a single nucleotide change resulting in a threonine-to-alanine substitution at amino acid 241. This residue is conserved in other serine-threonine protein kinases. These results identify this threonine as an important contact between catalytic and regulatory subunits but only a minor contact in substrate recognition.
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