ライフサイエンスコーパス: transformylase

1 (i) = 154 nM, IC(50) = 600 nM) against AICAR transformylase.

2 zyme of the purine biosynthesis pathway, GAR transformylase.

3 bservation that sulfasalazine inhibits AICAR transformylase.

4 an inhibitor of, glycinamide ribonucleotide transformylase.

5 ia coli and human glycinamide ribonucleotide transformylases.

6 -aminoimidazole-4-carboxamide ribonucleotide transformylase (347GG), methylenetetrahydrofolate reduct

7 parents targeted in earlier studies: two GAR transformylases (41% amino acid sequence identity), two

8 AICAR transformylase (5-aminoimidazole-4-carboxamide ribonucle

9 In yeast lacking MTHFS along with both AICAR transformylases, 5-CHO-THF was elevated 12-fold over wil

10 Identification of the AICAR transformylase active site and a proposed formyl transfe

11 Virtual screening of the human AICAR transformylase active site by use of AutoDock against th

12 Identification of the location of the AICAR transformylase active site was previously elucidated fro

13 Potent and selective inhibition of the AICAR transformylase active site, compared with other folate-d

14 on of the folate binding pocket of the AICAR transformylase active site.

15 Here we demonstrate that the transformylase activity of the Escherichia coli ArnA is

16 These indicated that the transformylase activity requires dimerization whereas th

17 -aminoimidazole-4-carboxamide ribonucleotide transformylase (AICAR Tfase) is evaluated with pH depend

18 Aminoimidazole-4-carboxamide ribonucleotide transformylase (AICAR Tfase), one of the two folate-depe

19 igate the specificity and mechanism of AICAR transformylase (AICAR Tfase).

20 aminoimidazole-4-carboxamide ribonucleotide transformylase (AICAR Tfase, residues 200-593)/IMPCH (AT

21 t enzyme, aminoimidazolecarboxamide ribotide transformylase (AICARTase).

22 e synthetase, and glycinamide ribonucleotide transformylase, all of which have known three-dimensiona

23 e synthase (GARS), phosphoribosylglycinamide transformylase (also abbreviated as GART), and phosphori

24 midazole-4-carboxamidoribonucleotide (AICAR) transformylase, an enzyme involved in de novo purine bio

25 ithin de novo purine biosynthesis, the AICAR transformylase and IMP cyclohydrolase activities of the

26 ATIC encompasses both AICAR transformylase and IMP cyclohydrolase activities that ar

27 unctional enzyme with folate-dependent AICAR transformylase and IMP cyclohydrolase activities that ca

28 vity of the bifunctional protein ATIC (AICAR transformylase and IMP cyclohydrolase) and is responsibl

29 -aminoimidazole-4-carboxamide ribonucleotide transformylase and inosine monophosphate cyclohydrolase

30 conservation around the active site of ArnA transformylase and other N-10-formyltetrahydrofolate-uti

31 erminal region of glycinamide ribonucleotide transformylase and several dinucleotide-dependent dehydr

32 -aminoimidazole-4-carboxamide ribonucleotide transformylase (ATIC) 347G were associated with methotre

33 dem repeats), amino imidazole ribonucleotide transformylase (ATIC) 347GG, and serine hydroxymethyltra

34 -aminoimidazole-4-carboxamide ribonucleotide transformylase (ATIC) and thymidylate synthase (TS).

35 sequence analyses, it is known that the PurT transformylase belongs to the ATP-grasp superfamily of p

36 to tetrahydrofolate and formate, whereas GAR transformylase catalyses the transfer of formyl from N10

37 osynthesis by MTX at the AICA ribonucleotide transformylase-catalyzed step may be related to the effi

38 amide ribonucleotide transformylase, or PurT transformylase, catalyzes an alternative formylation of

39 -resolution structural investigation of PurT transformylase complexed with various adenosine nucleoti

40 carboxyl-terminal region which, from the GAR transformylase crystal structure and labeling studies, i

41 We designate it the ArnA transformylase domain and describe its crystal structure

42 This reaction is catalyzed by the AICAR transformylase domain of the bifunctional enzyme AICAR t

43 AICAR is bound at the dimer interface of the transformylase domains and forms an extensive hydrogen b

44 timately bound at the dimer interface of the transformylase domains with the majority of AICAR moiety

45 s in catalysis by glycinamide ribonucleotide transformylase (EC 2.1.2.2).

46 talytic center of glycinamide ribonucleotide transformylase (EC 2.1.2.2).

47 cal to a group of glycinamide ribonucleotide transformylases (EC 2.1.2.2), resulted in the appearance

48 ycinamide ribonucleotide transformylase (GAR transformylase, EC 2.1.2.2) based on a steady-state and

49 aminoimidazole carboxamide ribotide (AICAR) transformylase forming bioactive dihydrofolate.

50 /or inhibitors of glycinamide ribonucleotide transformylase from chicken liver.

51 on X-ray crystallographic structures of PurT transformylase from E. coli: one form complexed with the

52 analyses, it has been demonstrated that PurT transformylase from Escherichia coli belongs to the ATP-

53 amide ribonucleotide transformylase, or PurT transformylase, functions in purine biosynthesis by cata

54 Glycinamide ribonucleotide transformylase (GAR Tfase) catalyzes the first of two fo

55 Glycinamide ribonucleotide transformylase (GAR Tfase) catalyzes the first of two fo

56 Glycinamide ribonucleotide transformylase (GAR Tfase) has been the target of anti-n

57 Glycinamide ribonucleotide transformylase (GAR Tfase) is a key folate-dependent enz

58 rd purine enzyme, glycinamide ribonucleotide transformylase (GAR Tfase) was monitored in live Escheri

59 hibitors (MAI) of glycinamide ribonucleotide transformylase (GAR Tfase), which incorporate key featur

60 coli purT encoded glycinamide ribonucleotide transformylase (GAR transformylase) serves as an alterna

61 Escherichia coli glycinamide ribonucleotide transformylase (GAR transformylase, EC 2.1.2.2) based on

62 Human glycinamide ribonucleotide transformylase (GART) (EC 2.1.2.2) is a validated target

63 ine inhibitors of glycinamide ribonucleotide transformylase (GART) are described.

64 Glycinamide ribonucleotide transformylase (GART) exhibits closely packed dimers in

65 In animals, the phosphoribosylglycinamide transformylase (GART) gene encodes a trifunctional prote

66 Glycinamide ribonucleotide transformylase (GART; 10-formyltetrahydrofolate:5'-phosp

67 Escherichia coli glycinamide ribonucleotide transformylase (GarTfase) disrupts the observed pH-depen

68 ia coli and human glycinamide ribonucleotide transformylase genes, which have only 50% identity on th

69 As such, AICAR transformylase has been proposed as a potential target f

70 me aminoimidazole-carboxamide ribonucleotide transformylase IMP cyclohydrolase, an enzyme not previou

71 idazole-4-carboxamide ribonucleotide (AICAR) transformylase/IMP cyclohydrolase (ATIC) is a bifunction

72 -Amino-4-imidazolecarboxamide ribonucleotide transformylase/IMP cyclohydrolase (ATIC) is a bifunction

73 The AICAR transformylase inhibitors BW1540 and BW2315 are sulfamid

74 e potent and specific non-folate-based AICAR transformylase inhibitors.

75 me aminoimidazole carboxamide ribonucleotide transformylase/inosine monophosphate cyclohydrolase (ATI

76 lase domain of the bifunctional enzyme AICAR transformylase/inosine monophosphate cyclohydrolase (ATI

77 me aminoimidazole carboxamide ribonucleotide transformylase/inosine monophosphate cyclohydrolase (ATI

78 -aminoimidazole-4-carboxamide ribonucleotide transformylase/inosine monophosphate cyclohydrolase, Ste

79 -aminoimidazole-4-carboxamide ribonucleotide transformylase) is a folate-dependent activity of the bi

80 idazole-4-carboxamide ribonucleotide (AICAR) transformylase isozymes (ADE16 and ADE17) resulted in a

81 -aminoimidazole-4-carboxamide ribonucleotide transformylase isozymes that catalyze the penultimate st

82 the PurT-encoded glycinamide ribonucleotide transformylase, or PurT transformylase, catalyzes an alt

83 PurT-encoded glycinamide ribonucleotide transformylase, or PurT transformylase, functions in pur

84 not formylated by the mitochondrial Met-tRNA transformylase preventing its function in initiation, an

85 2) The rate of the reverse transformylase reaction (6.7 s(-1)) is approximately 2-3

86 e determined the equilibrium constant of the transformylase reaction to be 0.024 +/- 0.001, showing t

87 drolase and glycinamide ribonucleotide (GAR) transformylase, respectively, catalyze similiar yet dist

88 of lysyl-tRNA synthetase and methionyl-tRNA transformylase results in partial formylation of the mut

89 ycinamide ribonucleotide transformylase (GAR transformylase) serves as an alternate enzyme in the pro

90 Specifically in PurT transformylase, the GAR substrate is anchored to the pro

91 hin 100- to 1000-fold of the native purN GAR transformylase validating the approach of constructing a