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Mechanism-based inactivation of mandelate racemase by propargylglycolate

Authors
Journal
Bioorganic & Medicinal Chemistry Letters
0960-894X
Publisher
Elsevier
Publication Date
Volume
2
Issue
11
Identifiers
DOI: 10.1016/s0960-894x(00)80523-5
Disciplines
  • Biology

Abstract

Abstract Propargylglycolate (2-hydroxy-3-butynoic acid) has been determined to be both a substrate and an inactivator of mandelate racemase. The partition ratio for racemization/inactivation has been estimated to be ∼17,000. Inactivation of the racemase appears to require the rapid covalent addition of 1 substrate molecule; however, a slower labeling process is observed that results in the attachment of up to 5 molecules of substrate per active site. The process is consistent with an enzyme-catalyzed rearrangement of the acetylenic substrate to an allenic-enol that affords 2-keto-3-butenoate as the ultimate electrophile.

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