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Science 1 April 1988:
Vol. 240. no. 4848, pp. 68 - 70
DOI: 10.1126/science.2832943
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Articles

Science, Vol 240, Issue 4848, 68-70
Copyright © 1988 by American Association for the Advancement of Science

articles

A mutation in the catalytic subunit of cAMP-dependent protein kinase that disrupts regulation

LR Levin, J Kuret, KE Johnson, S Powers, S Cameron, T Michaeli, M Wigler, and MJ Zoller

Cold Spring Harbor Laboratory, NY 11724.

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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