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Multisubstrate adduct inhibitors of glycinamide ribonucleotide transformylase: Synthetic and enzyme-assembled.

Authors
Journal
Tetrahedron
0040-4020
Publisher
Elsevier
Publication Date
Volume
47
Identifiers
DOI: 10.1016/s0040-4020(01)81773-7
Disciplines
  • Biology

Abstract

Abstract β-TGDDF, the displacement product of 2-thioacetamide ribonucleotide and N-10-(bromoacetyl)-5,8-dideazafolate, is a potent, slow, tight-binding, multisubstrate adduct inhibitor (MAI) of glycinamide ribonucleotide transformylase (GAR TFase: E.C. 2.1.2.2.). The mechanism of inhibition by this MAI and its derivatives are reported. In addition, a related series of MAIs formed from the interaction of glycinamide ribonucleotide (GAR) or its carbocyclic analog (carbo-β-GAR) and N-10-(bromoacetyl)-5,8-dideazafol with GAR TFase have been discovered and characterized. These latter enzyme assembled inhibitors represent a novel route to the inhibition of GAR TFase.

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