ライフサイエンスコーパス: dimethylbenzimidazole

1 thesis of N1-(5-phospho-alpha-D-ribosyl)-5,6-dimethylbenzimidazole.

2 e isotropic hyperfine coupling of the remote dimethylbenzimidazole (14)N nucleus in enzyme-bound vers

3 assigned to the remote (N1) nitrogen in the dimethylbenzimidazole alpha-axial ligand by using two in

4 rmediate N1-(5-phospho-alpha-D-ribosyl)-5, 6-dimethylbenzimidazole (also known as alpha-ribazole-5'-p

5 Increased flux through the 5,6-dimethylbenzimidazole and cobinamide (Cbi) activation br

6 Cobinamide, 5', 6'-dimethylbenzimidazole, and 2-aminopropanol did not repla

7 , which in adenosylcobalamin (AdoCbl) is 5,6-dimethylbenzimidazole, and in adenosylpseudocobalamin (A

8 First, a complex of CobT with 5,6-dimethylbenzimidazole, and second, a complex of CobT wit

9 Free dimethylbenzimidazole axial base-on cob(II)alamin was fo

10 ssessment of the degree of stabilization the dimethylbenzimidazole base provides for methyl transfer

11 s in the side chains that constitute the 5,6-dimethylbenzimidazole binding site.

12 Replacement of dimethylbenzimidazole by histidine may allow switching b

13 Dimethylbenzimidazole contributes approximately 0.6 kcal

14 Thus, dimethylbenzimidazole displacement appears to be an emer

15 y importing extracellular [p-Cre]Cba and 5,6-dimethylbenzimidazole (DMB) (the lower ligand of cobalam

16 hich transfers nitrogenous bases such as 5,6-dimethylbenzimidazole (DMB) and adenine, but cannot util

17 derivative that lacks the tethered base 5,6-dimethylbenzimidazole (DMB) and instead binds a water mo

18 t replacement of the intramolecular base 5,6-dimethylbenzimidazole (DMB) by a histidine residue from

19 he112 is critical in the displacement of 5,6-dimethylbenzimidazole (DMB) from its coordination bond w

20 CobT was cocrystallized with 5,6-dimethylbenzimidazole (DMB) in the space group P2(1)2(1)

21 led with (14)C at one particular atom of the dimethylbenzimidazole (DMB) moiety by exploiting idiosyn

22 ) and CobT(G171D) have less affinity for 5,6-dimethylbenzimidazole (DMB) or access of DMB to the acti

23 n various alpha-axial ligands, including 5,6-dimethylbenzimidazole (DMB) or adenine.

24 n Escherichia coli strain devoid of NaMN:5,6-dimethylbenzimidazole (DMB) phosphoribosyltransferase (C

25 Nicotinate mononucleotide (NaMN):5,6-dimethylbenzimidazole (DMB) phosphoribosyltransferase (C

26 ck CobT, the nicotinamide mononucleotide:5,6-dimethylbenzimidazole (DMB) phosphoribosyltransferase (E

27 is of the lower ligand of vitamin B(12), 5,6-dimethylbenzimidazole (DMB), is poorly understood.

28 es, Acetobacterium, which can synthesize 5,6-dimethylbenzimidazole (DMB), the lower ligand of cobalam

29 The synthesis of 5,6-dimethylbenzimidazole (DMB), the lower ligand of coenzym

30 The anaerobic biosynthesis of 5,6-dimethylbenzimidazole (DMB), the lower ligand of vitamin

31 lamin) or the lower ligand of cobalamin, 5,6-dimethylbenzimidazole (DMB).

32 to humans, has as its lower axial ligand 5,6-dimethylbenzimidazole (DMB).

33 erobic biosynthesis of the lower ligand, 5,6-dimethylbenzimidazole (DMB).

34 e base-off/His-off conformation, whereby the dimethylbenzimidazole group is replaced by a non-nitroge

35 nificantly different from the pKa of 3.7 for dimethylbenzimidazole in free AdoCbl.

36 ate mutants blocked in the synthesis of 5, 6-dimethylbenzimidazole in this bacterium.

37 We infer that dimethylbenzimidazole is also the alpha-axial ligand to

38 Upon binding to the protein, the usual dimethylbenzimidazole ligand is replaced by the imidazol

39 can be used to estimate the influence of the dimethylbenzimidazole ligand on both the thermodynamics

40 In this structure, the dimethylbenzimidazole ligand to the cobalt in free cobal

41 ase and methylmalonyl-coenzyme A mutase: The dimethylbenzimidazole ligand to the cobalt is displaced

42 The dimethylbenzimidazole ligand to the lower axial position

43 Cobinamides, with the B(12) 5,6-dimethylbenzimidazole loop removed, are excellent B(12)

44 The results identify the coenzyme's on-board dimethylbenzimidazole moiety as the alpha-axial ligand t

45 versible carbon skeleton rearrangements, the dimethylbenzimidazole moiety of the cofactor is not disp

46 h adenosylcobalamin enriched in (15)N in the dimethylbenzimidazole moiety show that the axial base of

47 from its precursors adenosylcobinamide, 5, 6-dimethylbenzimidazole, nicotinate mononucleotide, and GT

48 een displaced by a histidine ligand, and the dimethylbenzimidazole nucleotide "tail" is thrust into a

49 s of reaction of cobalamin, which contains a dimethylbenzimidazole nucleotide coordinated to the coba

50 > Arg, which map to the binding site for the dimethylbenzimidazole nucleotide substituent of adenosyl

51 to the cobalt in free methylcobalamin is the dimethylbenzimidazole nucleotide substituent of the corr

52 al position, and cobinamide, which lacks the dimethylbenzimidazole nucleotide, allows assessment of t

53 hase, which replaces the normal lower ligand dimethylbenzimidazole on binding of methylcobalamin to m

54 Nicotinate mononucleotide (NaMN):5,6-dimethylbenzimidazole phosphoribosyltransferase (CobT) f

55 Nicotinate mononucleotide:5,6-dimethylbenzimidazole phosphoribosyltransferase (CobT) f

56 thetic enzyme nicotinate-mononucleotide:5, 6-dimethylbenzimidazole phosphoribosyltransferase (CobT) f

57 ty for the nicotinic acid mononucleotide:5,6-dimethylbenzimidazole phosphoribosyltransferase enzyme (

58 tion position is occupied by the nucleotide, dimethylbenzimidazole ribose phosphate, that is attached

59 The data support an important role for the dimethylbenzimidazole tail in moving the cobalamin cofac

60 Cob(II)alamin binds with its dimethylbenzimidazole tail splayed into a side pocket an

61 fferent from that of cob(II)alamin, with the dimethylbenzimidazole tail tucked under the corrin ring,

62 a significant conformational change in which dimethylbenzimidazole, the lower axial ligand to cobalt

63 a significant conformational change in which dimethylbenzimidazole, the lower axial ligand to the cob

64 two residues, Phe91 and Trp93, displace 5,6-dimethylbenzimidazole, the lower nucleotide ligand base

65 hate) from nicotinate mononucleotide and 5,6-dimethylbenzimidazole, the reaction known to be catalyze

66 lay a role in catalyzing the displacement of dimethylbenzimidazole thereby facilitating the conformat

67 ide was 680 microM; the apparent Km for 5, 6-dimethylbenzimidazole was less than 10 microM.