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

Mobashery Shahriar | Zendy; Doughty Michael | Zendy; Kaiser E. T. | Zendy

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

Author(s) -

Mobashery Shahriar,

Doughty Michael,

Kaiser E. T.

Publication year - 1990

Publication title -

biopolymers

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.556

H-Index - 125

eISSN - 1097-0282

pISSN - 0006-3525

DOI - 10.1002/bip.360290118

Subject(s) - chemistry , protein subunit , peptide , dissociation constant , residue (chemistry) , protein kinase a , active site , biochemistry , enzyme , dissociation (chemistry) , stereochemistry , receptor , organic chemistry , gene

A peptide affinity inactivator, Ac‐Leu‐Arg‐Arg‐Ala‐(BrAc)Orn‐Leu‐Gly, was used as a tool to 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 −1 and a dissociation constant of 675 μ 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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