ライフサイエンスコーパス: formyl group

1 ituted at the aryl C3 position (ortho to the formyl group).

2 nly beta to the aldehyde carbonyl and in the formyl group.

3 hat the 2-vinyl group has been oxidized to a formyl group.

4 and beta to the aldehyde carbonyl and in the formyl group.

5 o has hydrogen-bonding interactions with the formyl group.

6 of the 5'-hydroxymethyl of riboflavin to the formyl group.

7 e in order to facilitate the transfer of the formyl group.

8 nvestigation to ortho'-substituted vinyl and formyl groups.

9 h sensitive functionalities-e.g. halides and formyl groups.

10 eloped for the synthesis of chlorins bearing formyl groups: (1) reaction of an acetal-substituted 1-a

11 ding pyrrole ring-opening products with an N-formyl group, 2-substituted anilines with different hydr

12 eliver 2,4-cyclohexadienones featuring a key formyl group and a quaternized carbon atom in good yield

13 sm for oxidation of the 2-vinyl group to a 2-formyl group and adds to the surprising array of chemica

14 etic version that features the transfer of a formyl group and hydride from an aldehyde substrate to a

15 on involved 1,2-addition of phthalide to the formyl group and intramolecular cyclization via substitu

16 de starting with intramolecular capture by a formyl group and termination by capture with HFIP solven

17 eme b by two chemical modifications, the C-8 formyl group and the C-2 hydroxyethylfarnesyl group.

18 A hydrogen bond between the formyl group and the exocyclic amine of the 3'-neighbor

19 sence of hydrogen bonding between the heme a formyl group and the R52 side chain, as suggested from c

20 id and vinyl alcohol vinylogues in which the formyl group and the vinyl group, respectively, were per

21 3.33) for hydrogen bond formation with the N-formyl group and with fMet, a model supported by MD simu

22 s to novel polycyclic scaffolds decorated by formyl groups and carboxylates suitable for subsequent m

23 Preactivation of the DDF formyl group appears to be key for catalysis, and struct

24 rved, and the 10 residues coordinating the N-formyl group are almost invariant.

25 In this study, the formyl group as a directing group gave the C4-arylated i

26 h is His in ePL kinase 1, interacts with the formyl group at C-4' of pyridoxal and may also determine

27 e introduction of a TIPS-ethynyl, acetyl, or formyl group at the 7-position was achieved using Pd-cat

28 54) of the intermediate domain transfers the formyl group between the catalytic domains of FDH.

29 Removal of the formyl group by a peptide deformylase renders the dipept

30 n the B ring of a tetrapyrrole molecule to a formyl group by chlorophyllide a oxygenase (CAO).

31 The resultant N-formyl group can be converted to N-H, NCH2OH, or NCH3.

32 The finding that the methyl and formyl groups channel the reaction regiospecificity in o

33 ucts arises from the photosensitizer: The N6-formyl group comes from oxidation of the methyl group an

34 peptide deformylase was shown to retain the formyl group confirming the physiological role of the de

35 in interacts with Arg 303 and Thr 301; its N-formyl group coordinates to Mg2+, and its hydroxyl group

36 We found that the 5-formyl group could increase duplex thermal stability and

37 el COTh building block, featuring functional formyl groups directly attached to the core's conjugated

38 Each porphyrin bears a formyl group distal to the surface attachment group for

39 e MTF, use N(10)-formyltetrahydrofolate as a formyl group donor.

40 cyanide alpha-carbon to protic solvents as a formyl group during imine formation is indicative of new

41 recombinantly overexpressed AT retains the N-formyl group (fAT), presumably due to incomplete N-formy

42 The requirement of an N-formyl group for channel activity, impermeability to cat

43 reate an oxyanion hole that helps orient the formyl group for nucleophilic attack by the 4-carboxamid

44 l domains: a hydrolase domain that removes a formyl group from 10-formyltetrahydrofolate and a NADP(+

45 ntose sugar and also catalyzes transfer of a formyl group from N-10-formyltetrahydrofolate to the 4'-

46 that catalyzes the removal of the N-terminal formyl group from nascent polypeptides in eubacteria.

47 zes the hydrolytic removal of the N-terminal formyl group from nascent ribosome-synthesized polypepti

48 enzyme that is responsible for removing the formyl group from nascently synthesized polypeptides in

49 a metal-dependent enzyme that removes the N-formyl group from newly synthesized bacterial proteins.

50 PDF) catalyzes the removal of the N-terminal formyl group from newly synthesized polypeptides in euba

51 zes the hydrolytic removal of the N-terminal formyl group from newly synthesized polypeptides in euba

52 lase catalyzes the removal of the N-terminal formyl group from newly synthesized polypeptides in euba

53 e deformylase catalyzes the removal of the N-formyl group from newly synthesized polypeptides in prok

54 atalytically active and able to remove the N-formyl group from several synthetic polypeptides, althou

55 ing of GTP but does not remove the resulting formyl group from the formamide.

56 experiments, suggests that the transfer of a formyl group from the formoxyborane occurs, which then l

57 zes the subsequent removal of the N-terminal formyl group from the majority of bacterial proteins.

58 enzyme in eubacteria for the removal of the formyl group from the N terminus of the nascent polypept

59 peptide deformylase (DEF), which removes the formyl group from the N-terminal formylmethionine in a p

60 oenzyme responsible for the removal of the N-formyl group from the N-terminal methionine of nascent p

61 ase (EC 3.5.1.31) catalyzes the removal of a formyl group from the N-termini of nascent ribosome-synt

62 HsPDF is capable of removing formyl groups from N-terminal methionines of newly synth

63 CH...O hydrogen bonds involving formyl groups have been invoked as a crucial factor cont

64 Prior syntheses of porphyrins bearing meso-formyl groups have generally employed the Vilsmeier form

65 of the chlorophylls and the formation of the formyl group in Chl f.

66 of two steps: (i) hydrolytic cleavage of the formyl group in the N-terminal catalytic domain, followe

67 Removal of the formyl group in these proteins by DEF would explain the

68 The disposition of the N5-formyl group in these structures indicates formation, at

69 he R201(5.38)XXXR205(5.42) (RGIIR) motif for formyl group interaction and receptor activation.

70 In a previous study we proposed that the formyl group is formed by an initial hydroxylation of th

71 The formyl group is held by a novel hydrogen bonding network

72 Our results showed that the 5-formyl group is located in the same plane as the cytosin

73 The formyl group is normally removed from the N-terminal Met

74 ked conformational change near the heme a(3) formyl group is postulated.

75 In this mechanism, it was not clear how the formyl group is transferred between the two catalytic do

76 rs between substrate and cofactor, while the formyl group is transferred from 10-formyltetrahydrofola

77 However, the biochemical provenance of this formyl group is unknown.

78 h formyl-methionine; however, the N-terminal formyl group is usually removed by peptide deformylase,

79 We report that the formyl group must be removed before the methionine resid

80 ance of the hydroxyl group of serine and the formyl group of 5-formyltetrahydrofolate in complexes of

81 because the hydroxymethyl group of 5hmC and formyl group of 5fC adopt restrained conformations throu

82 the methyl group of BChlide c or d into the formyl group of BChlide e or f This probably occurs by a

83 d (2)H) to determine the origin of the C2(1)-formyl group of Chl f and to verify whether Chl f is syn

84 h Q471, appears to be hydrogen-bonded to the formyl group of heme a in the X-ray structures.

85 the multidomain protein, HypX, converts the formyl group of N(10)-CHO-THF into water and CO, thereby

86 dence that purified HypX first transfers the formyl group of N(10)-formyl-THF to produce formyl-coenz

87 en atom derived from molecular oxygen on the formyl group of pyrrole B.

88 ria begins with a formylated methionine, the formyl group of the nascent polypeptide is removed by pe

89 iting reactivity differences between the two formyl groups of A,B-rings 9 to impart excellent regiose

90 me A by a further oxidation of a methyl to a formyl group on C-8.

91 A structure-activity study showed that the formyl group on position 1 and the bromine atom on posit

92 uced its pI by nearly 0.4, incorporating one formyl group onto the streptavidin homotetramer reduced

93 We found that the oxygen atom of the C2(1)-formyl group originates from molecular oxygen and not fr

94 atharanthine N-methyl group or a vindoline N-formyl group precludes Fe(III)-promoted coupling, wherea

95 ch, upon enzymatic removal of the N-terminal formyl group, rapidly release free thiols.

96 imidazoles, and pyrazoles substituted with a formyl group react with an aminocatalyst to generate an

97 ophorbine skeleton and bears a 7-methyl or 7-formyl group, respectively.

98 e a significant fraction of the BST with the formyl group retained.

99 hifted absorption maximum because of a C2(1)-formyl group substitution of Chl f However, the biochemi

100 Formyl group substitutions on the side chains of chlorop

101 the ortho'-substituent is a nonnucleophilic formyl group, the products include fused indanylnaphthal

102 construction of pyrroles bearing a 2-keto or formyl group through the intramolecular oxidative aza-an

103 d by (ii) NADP(+)-dependent oxidation of the formyl group to CO(2) in the C-terminal aldehyde dehydro

104 monocytogenes that lacked the ability to add formyl groups to nascent polypeptides.

105 The FAPY formyl group was positioned to form a hydrogen bond with

106 In addition to the normal formyl group, we find that the protein translational mac

107 ttached to lipid A is not derivatized with a formyl group, we postulate the existence of a deformylas

108 ble reason for this can be the effect of the formyl group, which remains intact, thus opening up poss

109 tion pathway that incorporates bioorthogonal formyl groups, which subsequently allows for the synthes