ライフサイエンスコーパス: deformylase

1 the zinc containing Escherichia coli peptide deformylase.

2 metal chelators strongly inhibit the E. coli deformylase.

3 a modest success with inhibitors of peptide deformylase.

4 essential prokaryotic gene encoding peptide deformylase.

5 te N-formyl-methionine processing by peptide deformylase.

6 ometric assay has been developed for peptide deformylase.

7 oup confirming the physiological role of the deformylase.

8 examine the sequence specificity of peptide deformylase.

9 he nascent polypeptide is removed by peptide deformylase.

10 be reconstituted in vitro from the denatured deformylase.

11 sitive method for kinetic studies of peptide deformylase.

12 nt, time-dependent inhibitors of the peptide deformylase.

13 g the processed forms of Arabidopsis peptide deformylase 1 and 2 (pAtDEF1 and 2, respectively) were e

14 fective in vitro against Arabidopsis peptide deformylase 1 and 2 activity, respectively.

15 ormyl group, we postulate the existence of a deformylase, acting later in the pathway.

16 Peptide deformylase activity was thought to be limited to riboso

17 Arabidopsis peptide deformylases had peptide deformylase activity with unique kinetic parameters that

18 e culture medium, thereby inhibiting peptide deformylase activity.

19 l formyl group is usually removed by peptide deformylase, an enzymatic activity requiring iron.

20 t of direct changes in interactions with the deformylase and Met aminopeptidase cannot be excluded.

21 nts that are inhibitors of bacterial peptide deformylase and UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylg

22 cription regulators, an apparent polypeptide deformylase, and a protein related to a virulence-associ

23 n the active site of all eubacterial peptide deformylases, and N-terminal extensions identifiable as

24 Deformylases are metalloproteases in bacteria, plants, a

25 here has been increasing interest in peptide deformylase as a potential target for antibacterial chem

26 Enzymatic exclusion of O2 from the deformylase assays renders the deformylase highly stable

27 ding sequence (def gene) of Escherichia coli deformylase behind a bacteriophage T7 promoter, we have,

28 of coordinated cysteine suggest that E. coli deformylase belongs to a new subfamily of metalloproteas

29 the zinc containing Escherichia coli peptide deformylase bound to the transition-state analogue, (S)-

30 In addition, active peptide deformylase can be reconstituted in vitro from the denat

31 Peptide deformylase catalyzes the removal of the N-formyl group

32 Peptide deformylase catalyzes the removal of the N-terminal form

33 ecies, we suggest that antibiotics targeting deformylase could have wide applicability.

34 Coexpression of the E. coli polypeptide deformylase (DEF), which removes the formyl group from t

35 eing a broad-specificity enzyme, the peptide deformylase deformylates different peptides at drastical

36 Peptide deformylase (EC 3.5.1.31) catalyzes the removal of a for

37 n has allowed the purification of > 50 mg of deformylase enzyme from each liter of cell culture.

38 fied iron-enriched form of S. aureus peptide deformylase enzyme retained high activity over many mont

39 ned to possess varying potencies against the deformylase enzyme revealed a linear correlation between

40 The deformylase exhibits strong preference for an L-methioni

41 In addition, the selectivity of peptide deformylase for the N-formyl over the N-acetyl group has

42 proximately 10 mg of pure, fully active Fe2+ deformylase from a liter of cells.

43 As an example, recombinant peptide deformylase from Bacillus subtilis was overexpressed, de

44 nd to be excellent substrates of the peptide deformylase from Escherichia coli (k(cat)/K(M) = 6.9 x 1

45 e inhibitors of purified recombinant peptide deformylase from Escherichia coli and Bacillus subtilis.

46 imum and the catalytic activity of a peptide deformylase from Escherichia coli.

47 recently solved structure of the eukaryotic deformylase from Plasmodium falciparum, a complete pictu

48 Both recombinant Arabidopsis peptide deformylases had peptide deformylase activity with uniqu

49 first crystal structure of Class II peptide deformylase has been determined.

50 A new, sensitive assay for the deformylase has been developed by measuring the amount o

51 A continuous assay for peptide deformylase has been developed using a formylated dipept

52 Escherichia coli extracts 3 decades ago, the deformylase has resisted all attempts of purification or

53 ntibiotics, inhibitors of bacterial peptidyl-deformylase, has been discovered by combining mechanism-

54 duct Sch 382583 (1), an inhibitor of peptide deformylase, has been synthesized in 16 steps from comme

55 fication and characterization of the peptide deformylase have remained a major challenge because this

56 f O2 from the deformylase assays renders the deformylase highly stable under otherwise identical cond

57 We describe here a new human peptide deformylase (Homo sapiens PDF, or HsPDF) that is localiz

58 The human homolog of peptide deformylase (HsPDF) resides in the mitochondria, along w

59 have, however, been able to overexpress this deformylase in Escherichia coli.

60 esults suggest an essential role for peptide deformylase in protein processing in all plant plastids.

61 GSK1322322 is a novel peptide deformylase inhibitor in the early phase of development

62 antibiotics, a glycylcycline, and a peptide deformylase inhibitor, a member of a new antibacterial c

63 eatment of Escherichia coli with the peptide deformylase inhibitor, actinonin, results in the expecte

64 Actinonin, a specific peptide deformylase inhibitor, was effective in vitro against Ar

65 The proteins for both deformylase-inhibitor complexes show basically the same

66 , guidelines for the design of high-affinity deformylase inhibitors are suggested.

67 sults will facilitate the design of specific deformylase inhibitors as potential antibacterial agents

68 l quinolones that have high potency, peptide deformylase inhibitors, and new lincosamide, oxazolidino

69 play a role in the design of general peptide deformylase inhibitors.

70 f oxidation of the catalytic Fe2+ ion of the deformylase into catalytically inactive Fe3+ ion by atmo

71 The deformylase is also capable of efficient deformylation o

72 Peptide deformylase is an essential Fe2+ metalloenzyme that cata

73 In vivo, the deformylase is capable of deformylating most of the poly

74 Purified deformylase is highly active toward N-formylated peptide

75 These results suggest that peptide deformylase is the likely molecular target responsible f

76 inhibitory activity toward Escherichia coli deformylase (K(I) = 0.67 nM) and antibacterial activity

77 otes, PurU (10-formyl tetrahydrofolate [THF] deformylase) metabolizes 10-formyl THF to formate and TH

78 recombinant form of Escherichia coli peptide deformylase (PDF(Ec)) via isothermal titration microcalo

79 Peptide deformylase (PDF) catalyzes the hydrolytic removal of th

80 Peptide deformylase (PDF) catalyzes the hydrolytic removal of th

81 Peptide deformylase (PDF) catalyzes the removal of the N-termina

82 Peptide deformylase (PDF) catalyzes the subsequent removal of th

83 When the streptococcal polypeptide deformylase (PDF) gene (def1, encoding PDF) was placed u

84 Peptide deformylase (PDF) has been identified as a promising ant

85 Peptide deformylase (PDF) has received considerable attention du

86 Polypeptide deformylase (PDF) is a highly conserved bacterial enzyme

87 Polypeptide deformylase (PDF) is a novel broad-spectrum antibacteria

88 Peptide deformylase (PDF) is among the few antibacterial targets

89 Peptide deformylase (PDF) is an enzyme that is responsible for r

90 Polypeptide deformylase (PDF) is an essential bacterial metalloenzym

91 Peptide deformylase (PDF) is essential in prokaryotes and absent

92 able promoter region of the gene for peptide deformylase (PDF), a metal-dependent enzyme that removes

93 rminal Met residue of the peptide by peptide deformylase (PDF).

94 plication to kinetic characterization of the deformylase, pH profile studies, and enzyme inhibition a

95 ation for the protection of the epitope from deformylases present in the bacterial cell and suggests

96 ctive species, which covalently modifies the deformylase protein, most likely by oxidizing cysteine-9

97 Peptide deformylase proteins (PDFs) participate in the N-termina

98 The deformylase reaction is conveniently monitored on a UV-V

99 Removal of the formyl group by a peptide deformylase renders the dipeptide product, which contain

100 Limited treatment with the Escherichia coli deformylase resulted in the deformylation of those pepti

101 alciparum, a complete picture of the peptide deformylase structure and function relationship is emerg

102 employs a novel class of peptide mimetics as deformylase substrates which, upon enzymatic removal of

103 tylase may have an analogous function to the deformylase that generates undecaprenyl phosphate-4-amin

104 eir protein biosynthetic mechanisms, peptide deformylase, the bacterial enzyme responsible for deform

105 n of effective antibiotics targeting peptide deformylase, the structures of the protein-inhibitor com

106 d, three sample mononuclear enzymes, peptide deformylase, threonine dehydrogenase, and cytosine deami

107 sment of the catalytic properties of peptide deformylase using a series of synthetic N-formylated pep

108 The deformylase was also shown to exhibit esterase activity.

109 ocyclic, peptidomimetic inhibitor of peptide deformylase was designed by covalently cross-linking the

110 rotein expressed in a strain lacking peptide deformylase was shown to retain the formyl group confirm

111 rapid method to study kinetic properties of deformylases without the use of any coupling enzymes.