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1 at least a modest success with inhibitors of peptide deformylase.
2 incomplete N-formyl-methionine processing by peptide deformylase.
3 s of the essential prokaryotic gene encoding peptide deformylase.
4 ctrophotometric assay has been developed for peptide deformylase.
5 atically examine the sequence specificity of peptide deformylase.
6 oup of the nascent polypeptide is removed by peptide deformylase.
7  and sensitive method for kinetic studies of peptide deformylase.
8  as potent, time-dependent inhibitors of the peptide deformylase.
9 tion of the zinc containing Escherichia coli peptide deformylase.
10  encoding the processed forms of Arabidopsis peptide deformylase 1 and 2 (pAtDEF1 and 2, respectively
11 , was effective in vitro against Arabidopsis peptide deformylase 1 and 2 activity, respectively.
12                                              Peptide deformylase activity was thought to be limited t
13 mbinant Arabidopsis peptide deformylases had peptide deformylase activity with unique kinetic paramet
14 on in the culture medium, thereby inhibiting peptide deformylase activity.
15 -terminal formyl group is usually removed by peptide deformylase, an enzymatic activity requiring iro
16 rial agents that are inhibitors of bacterial peptide deformylase and UDP-3-O-(R-3-hydroxymyristoyl)-N
17  found in the active site of all eubacterial peptide deformylases, and N-terminal extensions identifi
18 minus, there has been increasing interest in peptide deformylase as a potential target for antibacter
19 alt and the zinc containing Escherichia coli peptide deformylase bound to the transition-state analog
20                          In addition, active peptide deformylase can be reconstituted in vitro from t
21                                              Peptide deformylase catalyzes the removal of the N-formy
22                                              Peptide deformylase catalyzes the removal of the N-termi
23 espite being a broad-specificity enzyme, the peptide deformylase deformylates different peptides at d
24                                              Peptide deformylase (EC 3.5.1.31) catalyzes the removal
25 The purified iron-enriched form of S. aureus peptide deformylase enzyme retained high activity over m
26              In addition, the selectivity of peptide deformylase for the N-formyl over the N-acetyl g
27                   As an example, recombinant peptide deformylase from Bacillus subtilis was overexpre
28  and found to be excellent substrates of the peptide deformylase from Escherichia coli (k(cat)/K(M) =
29 eversible inhibitors of purified recombinant peptide deformylase from Escherichia coli and Bacillus s
30 e pH optimum and the catalytic activity of a peptide deformylase from Escherichia coli.
31                 Both recombinant Arabidopsis peptide deformylases had peptide deformylase activity wi
32      The first crystal structure of Class II peptide deformylase has been determined.
33                       A continuous assay for peptide deformylase has been developed using a formylate
34 ural product Sch 382583 (1), an inhibitor of peptide deformylase, has been synthesized in 16 steps fr
35 er, purification and characterization of the peptide deformylase have remained a major challenge beca
36                 We describe here a new human peptide deformylase (Homo sapiens PDF, or HsPDF) that is
37                         The human homolog of peptide deformylase (HsPDF) resides in the mitochondria,
38    The results suggest an essential role for peptide deformylase in protein processing in all plant p
39                        GSK1322322 is a novel peptide deformylase inhibitor in the early phase of deve
40  peptide antibiotics, a glycylcycline, and a peptide deformylase inhibitor, a member of a new antibac
41  that treatment of Escherichia coli with the peptide deformylase inhibitor, actinonin, results in the
42                        Actinonin, a specific peptide deformylase inhibitor, was effective in vitro ag
43 her novel quinolones that have high potency, peptide deformylase inhibitors, and new lincosamide, oxa
44 ich may play a role in the design of general peptide deformylase inhibitors.
45                                              Peptide deformylase is an essential Fe2+ metalloenzyme t
46                   These results suggest that peptide deformylase is the likely molecular target respo
47 tituted recombinant form of Escherichia coli peptide deformylase (PDF(Ec)) via isothermal titration m
48                                              Peptide deformylase (PDF) catalyzes the hydrolytic remov
49                                              Peptide deformylase (PDF) catalyzes the hydrolytic remov
50                                              Peptide deformylase (PDF) catalyzes the removal of the N
51                                              Peptide deformylase (PDF) catalyzes the subsequent remov
52                                              Peptide deformylase (PDF) has been identified as a promi
53                                              Peptide deformylase (PDF) has received considerable atte
54                                              Peptide deformylase (PDF) is among the few antibacterial
55                                              Peptide deformylase (PDF) is an enzyme that is responsib
56                                              Peptide deformylase (PDF) is essential in prokaryotes an
57 e presumable promoter region of the gene for peptide deformylase (PDF), a metal-dependent enzyme that
58 the N-terminal Met residue of the peptide by peptide deformylase (PDF).
59                                              Peptide deformylase proteins (PDFs) participate in the N
60             Removal of the formyl group by a peptide deformylase renders the dipeptide product, which
61 modium falciparum, a complete picture of the peptide deformylase structure and function relationship
62 er in their protein biosynthetic mechanisms, peptide deformylase, the bacterial enzyme responsible fo
63 he design of effective antibiotics targeting peptide deformylase, the structures of the protein-inhib
64    Indeed, three sample mononuclear enzymes, peptide deformylase, threonine dehydrogenase, and cytosi
65 he assessment of the catalytic properties of peptide deformylase using a series of synthetic N-formyl
66   A macrocyclic, peptidomimetic inhibitor of peptide deformylase was designed by covalently cross-lin
67 porter protein expressed in a strain lacking peptide deformylase was shown to retain the formyl group

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