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Inactivation of the catalytic subunit of bovine cAMP-dependent protein kinase by a peptide-based affinity inactivator

✍ Scribed by Shahriar Mobashery; Michael Doughty; E. T. Kaiser

Publisher: Wiley (John Wiley & Sons)
Year: 1990
Tongue: English
Weight: 610 KB
Volume: 29
Category: Article
ISSN: 0006-3525
DOI: 10.1002/bip.360290118

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✦ Synopsis

A peptide affinity inactivator, Ac-Leu-Arg-Arg-Ala-(BrAc)Om-Leu-Gly, was used as a tool t o probe for active site residues in the catalytic subunit of bovine CAMP-dependent protein kinase. The peptide inactivated the catalytic subunit in an active site-directed and monophasic manner with a first-order rate constant of 0.03 min-' and a dissociation constant of 675 p M . Studies with radioactive peptide indicated that approximately one equivalent of peptide was incorporated into each protein molecule. Protein sequencing identified the modified residue as Cys-199. A possible location for Cys-199 within the active site is suggested.

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