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1 y direct nucleophilic attack by the amine of glycinamide ribonucleotide.
2 es ranging from 7.4 to 23.6 times the Km for glycinamide ribonucleotide.
3 alues ranged from 21 to 118 times the Km for glycinamide ribonucleotide.
4 Vmax values comparable to that obtained with glycinamide ribonucleotide, although the Km values range
5                                      Several glycinamide ribonucleotide analogs have been prepared an
6                                              Glycinamide ribonucleotide analogs include side chain mo
7 0-formyl-5,8-dideazafolate cosubstrate and a glycinamide ribonucleotide analogue, hydroxyacetamide ri
8 ormyl dideazafolate and dideazafolate or for glycinamide ribonucleotide and formyl glycinamide ribonu
9                           Several analogs of glycinamide ribonucleotide and phosphoribosylamine have
10 or for glycinamide ribonucleotide and formyl glycinamide ribonucleotide are similar.
11 f GAR Tfase with its natural substrate, beta-glycinamide ribonucleotide (beta-GAR), at pH 8.5 confirm
12         The ionization of the amino group of glycinamide ribonucleotide both as a free and as a bound
13           The product analog DDATHF and beta-glycinamide ribonucleotide bound to enzyme equally well
14 ver, the O-phosphonate analog of carbocyclic glycinamide ribonucleotide did support enzymatic activit
15 ng the phosphonate derivative of carbocyclic glycinamide ribonucleotide, did not serve as substrates,
16 p of the purine biosynthetic pathway, formyl glycinamide ribonucleotide (FGAR) amidotransferase, also
17                                              Glycinamide ribonucleotide formyl transferase (GARFTase)
18 cted against dihydrofolate reductase (DHFR), glycinamide ribonucleotide formyltransferase (GARFT), 5-
19 including dihydrofolate reductase (DHFR) and glycinamide ribonucleotide formyltransferase (GARFT).
20 eceptor (FR) cellular uptake specificity and glycinamide ribonucleotide formyltransferase (GARFTase)
21                                              Glycinamide ribonucleotide formyltransferase (GARFTase)
22 erine hydroxymethyl transferase (SHMT) 2 and glycinamide ribonucleotide formyltransferase (GARFTase)
23 mino-4-imidazolecarboxamide, suggesting that glycinamide ribonucleotide formyltransferase (GARFTase)
24                 All four analogues inhibited glycinamide ribonucleotide formyltransferase (GARFTase).
25 of de novo purine nucleotide biosynthesis at glycinamide ribonucleotide formyltransferase (GARFTase).
26 ucleotide formyltransferase (AICARFTase) and glycinamide ribonucleotide formyltransferase (GARFTase).
27 ne synthesis because of potent inhibition of glycinamide ribonucleotide formyltransferase (GART) but
28 idazole ribonucleotide synthetase (AIRS) and glycinamide ribonucleotide formyltransferase (GART) enzy
29                                    The mouse glycinamide ribonucleotide formyltransferase (GART) locu
30 ne synthesis by folate analogs inhibitory to glycinamide ribonucleotide formyltransferase (GART).
31  (PurN) and the C-terminal fragment of human glycinamide ribonucleotide formyltransferase (hGART) was
32  the N-terminal fragment of Escherichia coli glycinamide ribonucleotide formyltransferase (PurN) and
33  tested this methodology on Escherichia coli glycinamide ribonucleotide formyltransferase (PurN) and,
34 glutamate to recombinant trifunctional mouse glycinamide ribonucleotide formyltransferase (rmGARFT) w
35 ity was identified as the dual inhibition of glycinamide ribonucleotide formyltransferase and, likely
36                          C1 and C2 inhibited glycinamide ribonucleotide formyltransferase in de novo
37 Compounds 7 and 11 were potent inhibitors of glycinamide ribonucleotide formyltransferase in de novo
38                                              Glycinamide ribonucleotide formyltransferase was the pri
39 nzymes, methionyl-tRNA-formyltransferase and glycinamide ribonucleotide formyltransferase, but, unexp
40 l extension that is not found in the E. coli glycinamide ribonucleotide formyltransferase, which, lik
41 ructure of ArnA based on its similarity with glycinamide ribonucleotide formyltransferase.
42 ependent enzyme in de novo purine synthesis, glycinamide ribonucleotide formyltransferase.
43     SCRATCHY libraries were created from the glycinamide-ribonucleotide formyltransferase (GART) gene
44 ase, catalyzes an alternative formylation of glycinamide ribonucleotide (GAR) in the de novo pathway
45 rN, N10-formyltetrahydrofolate hydrolase and glycinamide ribonucleotide (GAR) transformylase, respect
46  of phosphoribosylamine, glycine, and ATP to glycinamide ribonucleotide (GAR), ADP, and Pi.
47                           Furthermore, alpha-glycinamide ribonucleotide had no effect on enzyme activ
48               Several carbocyclic analogs of glycinamide ribonucleotide, including the phosphonate de
49 ism was implicated in which the enzyme binds glycinamide ribonucleotide or formyl dideazafolate produ
50                                              Glycinamide ribonucleotide synthetase (GAR-syn) catalyze
51 sylpyrophosphate amidotransferase (GPAT) and glycinamide ribonucleotide synthetase (GARS) from Aquife
52 re catalyzed by a trifunctional protein with glycinamide ribonucleotide synthetase (GARS), aminoimida
53 een prepared and evaluated as substrates for glycinamide ribonucleotide synthetase purified from chic
54 iosynthesis by catalyzing the formylation of glycinamide ribonucleotide through a catalytic mechanism
55 tive site residues and loops in catalysis by glycinamide ribonucleotide transformylase (EC 2.1.2.2).
56 esidue within 6 A of the catalytic center of glycinamide ribonucleotide transformylase (EC 2.1.2.2).
57                                              Glycinamide ribonucleotide transformylase (GAR Tfase) ca
58                                              Glycinamide ribonucleotide transformylase (GAR Tfase) ca
59                                              Glycinamide ribonucleotide transformylase (GAR Tfase) ha
60                                              Glycinamide ribonucleotide transformylase (GAR Tfase) is
61 lization pattern of the third purine enzyme, glycinamide ribonucleotide transformylase (GAR Tfase) wa
62    Multisubstrate adduct inhibitors (MAI) of glycinamide ribonucleotide transformylase (GAR Tfase), w
63 tic scheme is presented for Escherichia coli glycinamide ribonucleotide transformylase (GAR transform
64            The Escherichia coli purT encoded glycinamide ribonucleotide transformylase (GAR transform
65                                        Human glycinamide ribonucleotide transformylase (GART) (EC 2.1
66 ,6-diamino-4(3H)-oxopyrimidine inhibitors of glycinamide ribonucleotide transformylase (GART) are des
67                                              Glycinamide ribonucleotide transformylase (GART) exhibit
68                                              Glycinamide ribonucleotide transformylase (GART; 10-form
69 n in the dimer interface of Escherichia coli glycinamide ribonucleotide transformylase (GarTfase) dis
70 shows similarity to the N-terminal region of glycinamide ribonucleotide transformylase and several di
71 evaluated as substrates and/or inhibitors of glycinamide ribonucleotide transformylase from chicken l
72  fragments of the Escherichia coli and human glycinamide ribonucleotide transformylase genes, which h
73 minoimidazole ribonucleotide synthetase, and glycinamide ribonucleotide transformylase, all of which
74                                 PurT-encoded glycinamide ribonucleotide transformylase, or PurT trans
75        In Escherichia coli, the PurT-encoded glycinamide ribonucleotide transformylase, or PurT trans
76 either a substrate for, nor an inhibitor of, glycinamide ribonucleotide transformylase.
77 03), which is 24-30% identical to a group of glycinamide ribonucleotide transformylases (EC 2.1.2.2),
78 ion libraries for Escherichia coli and human glycinamide ribonucleotide transformylases.
79 ion, identified PurN heterodimers capable of glycinamide ribonucleotide transformylation.
80 nhibitors of the enzyme, competitive against glycinamide ribonucleotide, with Ki values ranging from