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Irreversible inhibition of aldolase by a phosphorylated alpha-dicarbonyl compound.

Authors
Type
Published Article
Journal
Journal of enzyme inhibition and medicinal chemistry
Publication Date
Volume
23
Issue
1
Pages
21–27
Identifiers
DOI: 10.1080/14756360701383718
PMID: 18341248
Source
Medline
License
Unknown

Abstract

The preparation of a phosphorylated alpha-dicarbonyl compound designed to specifically react with arginine residues of enzymes accepting phosphorylated compounds as effectors is reported, and shown to inhibit rabbit muscle aldolase in a time-dependent and irreversible manner. This irreversible inhibition occured in a buffer devoid of borate ions, suggesting that the presence of the phosphate moiety contributes in the stabilization of the adduct formed with arginine residues. Under the same conditions, the metalloenzyme iron superoxide dismutase, in which an arginine is known to be critical for the catalytic function, is not significantly inhibited.

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