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1 either a substrate for, nor an inhibitor of, glycinamide ribonucleotide transformylase.
2 ion libraries for Escherichia coli and human glycinamide ribonucleotide transformylases.
3 minoimidazole ribonucleotide synthetase, and glycinamide ribonucleotide transformylase, all of which
4 shows similarity to the N-terminal region of glycinamide ribonucleotide transformylase and several di
5 tive site residues and loops in catalysis by glycinamide ribonucleotide transformylase (EC 2.1.2.2).
6 esidue within 6 A of the catalytic center of glycinamide ribonucleotide transformylase (EC 2.1.2.2).
7 03), which is 24-30% identical to a group of glycinamide ribonucleotide transformylases (EC 2.1.2.2),
8 evaluated as substrates and/or inhibitors of glycinamide ribonucleotide transformylase from chicken l
13 lization pattern of the third purine enzyme, glycinamide ribonucleotide transformylase (GAR Tfase) wa
14 Multisubstrate adduct inhibitors (MAI) of glycinamide ribonucleotide transformylase (GAR Tfase), w
15 tic scheme is presented for Escherichia coli glycinamide ribonucleotide transformylase (GAR transform
18 ,6-diamino-4(3H)-oxopyrimidine inhibitors of glycinamide ribonucleotide transformylase (GART) are des
21 n in the dimer interface of Escherichia coli glycinamide ribonucleotide transformylase (GarTfase) dis
22 fragments of the Escherichia coli and human glycinamide ribonucleotide transformylase genes, which h
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