TY - JOUR
T1 - Multisubstrate adduct inhibitors of glycinamide ribonucleotide transformylase
T2 - Synthetic and enzyme-assembled.
AU - Inglese, James
AU - Benkovic, Stephen J.
PY - 1991
Y1 - 1991
N2 - 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.
AB - 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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U2 - 10.1016/S0040-4020(01)81773-7
DO - 10.1016/S0040-4020(01)81773-7
M3 - Article
AN - SCOPUS:0025974512
SN - 0040-4020
VL - 47
SP - 2351
EP - 2364
JO - Tetrahedron
JF - Tetrahedron
IS - 14-15
ER -