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1 transferase and, likely, AICA ribonucleotide formyltransferase.
2 s similarity with glycinamide ribonucleotide formyltransferase.
3 is highly homologous to methionyl-tRNA(f)Met formyltransferase.
4 purine synthesis, glycinamide ribonucleotide formyltransferase.
5 -aminoimidazole-4-carboxamide ribonucleotide formyltransferase.
6 ing purT (encoding phosphoribosylglycinamide formyltransferase 2 in the purine synthesis pathway) was
7 on aminoimidazole carboxamide ribonucleotide formyltransferase, 5,10-methylenetetrahydrofolate dehydr
8 ely the release of tetrahydrofolate from the formyltransferase active site or a conformational change
10 ymes phosphoribosylaminoimidazolecarboxamide formyltransferase (AICARFT) and serine hydroxymethyltran
11 aminoimidazole-4-carboxamide ribonucleotide formyltransferase (AICARFT), an enzyme in the purine bio
12 -aminoimidazole-4-carboxamide ribonucleotide formyltransferase (AICARFT), and thymidylate synthase (T
13 sting inhibition of both AICA ribonucleotide formyltransferase (AICARFTase) and glycinamide ribonucle
14 ls, aminoimidazolecarboxamide ribonucleotide formyltransferase (AICART), the second folate-dependent
16 iron-regulated fxbA gene encodes a putative formyltransferase, an essential enzyme in the exochelin
17 fold as the related enzymes, methionyl-tRNA-formyltransferase and glycinamide ribonucleotide formylt
18 zole carboxamide ribonucleotide, between the formyltransferase and the cyclohydrolase active sites.
19 ual inhibition of glycinamide ribonucleotide formyltransferase and, likely, AICA ribonucleotide formy
20 yltransferase and glycinamide ribonucleotide formyltransferase, but, unexpectedly, the structural sim
21 port the crystal structure of the N-terminal formyltransferase domain in a complex with uridine monop
22 ntity with Escherichia coli L-methionyl-tRNA formyltransferase (EC 2.1.2.9), was expressed as a solub
23 etrahydrofolate:5'-phosphoribosylglycinamide formyltransferase, EC 2.1.2.2), an essential enzyme in d
24 hydrofolate dehydrogenase and methionyl-tRNA-formyltransferase extends to the C terminus of both prot
25 ed equidistantly from the active site of the formyltransferase (FhcD) and metallo-hydrolase (FhcA).
28 reductase (DHFR), glycinamide ribonucleotide formyltransferase (GARFT), 5-aminoimidazole-4-carboxamid
30 , suggesting that glycinamide ribonucleotide formyltransferase (GARFTase) in de novo purine biosynthe
33 rase (SHMT) 2 and glycinamide ribonucleotide formyltransferase (GARFTase) structures, and published X
37 ent inhibition of glycinamide ribonucleotide formyltransferase (GART) but do not induce detectable le
39 created from the glycinamide-ribonucleotide formyltransferase (GART) genes from Escherichia coli (pu
42 fragment of human glycinamide ribonucleotide formyltransferase (hGART) was prepared and successfully
44 al role in interfacing the coenzyme with the formyltransferase/hydrolase complex, an enzyme that gene
45 aminoimidazole- 4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase (AICARFT/IMPCHase).
46 -aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase (ATIC), a bifunctio
47 -aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase (ATIC), a single en
48 tein phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase (PurH, EC 2.1.2.3/3
49 -aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase-mediated glucose tr
50 ent inhibitors of glycinamide ribonucleotide formyltransferase in de novo purine biosynthesis in KB h
51 and C2 inhibited glycinamide ribonucleotide formyltransferase in de novo purine nucleotide biosynthe
52 -aminoimidazole-4-carboxamide ribonucleotide formyltransferase/inosine monophosphate cyclohydrolase (
53 -aminoimidazole-4-carboxamide ribonucleotide formyltransferase/inosine monophosphate cyclohydrolase (
54 -aminoimidazole-4-carboxamide ribonucleotide formyltransferase/inosine monophosphate cyclohydrolase (
55 locus, encoding mitochondrial methionyl-tRNA formyltransferase, lack detectable fMet-tRNAfMet but exh
56 ordantly, in vivo ablation of methionyl-tRNA formyltransferase (MTF) in Escherichia coli increases th
57 e manner the Escherichia coli methionyl-tRNA formyltransferase (MTF) in the cytoplasm of the yeast Sa
58 f initiator methionyl-tRNA by methionyl-tRNA formyltransferase (MTF) is important for initiation of p
59 f initiator methionyl-tRNA by methionyl-tRNA formyltransferase (MTF) is important for initiation of p
60 methionyl-tRNA (Met-tRNA) by methionyl-tRNA formyltransferase (MTF) is important for the initiation
61 f initiator methionyl-tRNA by methionyl-tRNA formyltransferase (MTF) is important for the initiation
62 f initiator methionyl-tRNA by methionyl-tRNA formyltransferase (MTF) is important for the initiation
63 ionyl-tRNA (Met-tRNA(Met)) by methionyl-tRNA formyltransferase (MTF) is important for translation ini
64 tion reaction is catalyzed by methionyl-tRNA formyltransferase (MTF) located in mitochondria and uses
65 f initiator methionyl-tRNA by methionyl-tRNA formyltransferase (MTF; EC 2.1.2.9) is important for the
66 n loop present in eubacterial methionyl-tRNA formyltransferases (MTF) is critical for specific recogn
67 sis of 10-formyl-THF, and the methionyl-tRNA formyltransferase (open reading frame YBL013W; designate
68 g aminoacyl-tRNA synthetases, methionyl-tRNA formyltransferase, or IF2, we identified the steps limit
70 Escherichia coli glycinamide ribonucleotide formyltransferase (PurN) and the C-terminal fragment of
71 Escherichia coli glycinamide ribonucleotide formyltransferase (PurN) and, by genetic selection, iden
73 ifunctional mouse glycinamide ribonucleotide formyltransferase (rmGARFT) was studied by equilibrium d
75 nd in the E. coli glycinamide ribonucleotide formyltransferase, which, like MTF, use N(10)-formyltetr