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S-N Transfer and Dual Acetylation in the S-Acetylation and N-Acetylation of 3-Phosphoglyceraldehyde Dehydrogenase by Substrates

Jane Harting Park 1, C. F. Agnello 1, and Elizabeth Mathew 1

From the 1 From the Department of Physiology, Vanderbilt University Medical School, Nashville, Tennessee 37203

Acetyl phosphate or p-nitrophenyl acetate acetylates a specific cysteine residue in 3-phosphoglyceraldehyde dehydrogenase to give an active acetyl-enzyme compound. By raising the pH above 7.0, the acetyl group migrates to the egr-amino group of a lysine residue to form an enzymatically inactive compound. This S-N acetyl transfer is the principal route for N-acetylation of the lysine residue on the dehydrogenase. A number of considerations suggest that the cysteine and lysine residues are in close proximity although they are not near neighbors in a single peptide chain.

Submitted on November 30, 1965


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Copyright © 1966 by the American Society for Biochemistry and Molecular Biology.
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