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1 at least a modest success with inhibitors of peptide deformylase.
2 s of the essential prokaryotic gene encoding peptide deformylase.
3 incomplete N-formyl-methionine processing by 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           Similar results were obtained with peptide deformylase, another essential enzyme of the mon
19 minus, there has been increasing interest in peptide deformylase as a potential target for antibacter
20 alt and the zinc containing Escherichia coli peptide deformylase bound to the transition-state analog
21                          In addition, active peptide deformylase can be reconstituted in vitro from t
22                                              Peptide deformylase catalyzes the removal of the N-formy
23                                              Peptide deformylase catalyzes the removal of the N-termi
24 espite being a broad-specificity enzyme, the peptide deformylase deformylates different peptides at d
25                                              Peptide deformylase (EC 3.5.1.31) catalyzes the removal
26 The purified iron-enriched form of S. aureus peptide deformylase enzyme retained high activity over m
27              In addition, the selectivity of peptide deformylase for the N-formyl over the N-acetyl g
28                   As an example, recombinant peptide deformylase from Bacillus subtilis was overexpre
29  and found to be excellent substrates of the peptide deformylase from Escherichia coli (k(cat)/K(M) =
30 eversible inhibitors of purified recombinant peptide deformylase from Escherichia coli and Bacillus s
31 e pH optimum and the catalytic activity of a peptide deformylase from Escherichia coli.
32                 Both recombinant Arabidopsis peptide deformylases had peptide deformylase activity wi
33      The first crystal structure of Class II peptide deformylase has been determined.
34                       A continuous assay for peptide deformylase has been developed using a formylate
35 ural product Sch 382583 (1), an inhibitor of peptide deformylase, has been synthesized in 16 steps fr
36 er, purification and characterization of the peptide deformylase have remained a major challenge beca
37                 We describe here a new human peptide deformylase (Homo sapiens PDF, or HsPDF) that is
38                         The human homolog of peptide deformylase (HsPDF) resides in the mitochondria,
39    The results suggest an essential role for peptide deformylase in protein processing in all plant p
40                        GSK1322322 is a novel peptide deformylase inhibitor in the early phase of deve
41  peptide antibiotics, a glycylcycline, and a peptide deformylase inhibitor, a member of a new antibac
42  that treatment of Escherichia coli with the peptide deformylase inhibitor, actinonin, results in the
43                        Actinonin, a specific peptide deformylase inhibitor, was effective in vitro ag
44 her novel quinolones that have high potency, peptide deformylase inhibitors, and new lincosamide, oxa
45 ich may play a role in the design of general peptide deformylase inhibitors.
46                   We show that DefA, a minor peptide deformylase, inhibits the activity of BY-kinase
47                                              Peptide deformylase is an essential Fe2+ metalloenzyme t
48                   These results suggest that peptide deformylase is the likely molecular target respo
49 tituted recombinant form of Escherichia coli peptide deformylase (PDF(Ec)) via isothermal titration m
50 onin is the most potent natural inhibitor of peptide deformylase (PDF) and exerts antimicrobial and h
51  it obstructs their ensuing deformylation by peptide deformylase (PDF) and hydrolysis by methionyl am
52 ria, NME is mediated by 2 essential enzymes, peptide deformylase (PDF) and methionine aminopeptidase
53                                              Peptide deformylase (PDF) catalyzes the hydrolytic remov
54                                              Peptide deformylase (PDF) catalyzes the hydrolytic remov
55                                              Peptide deformylase (PDF) catalyzes the removal of the N
56                                              Peptide deformylase (PDF) catalyzes the subsequent remov
57                                              Peptide deformylase (PDF) has been identified as a promi
58                                              Peptide deformylase (PDF) has received considerable atte
59                                              Peptide deformylase (PDF) is among the few antibacterial
60                                              Peptide deformylase (PDF) is an enzyme that is responsib
61                                              Peptide deformylase (PDF) is essential in prokaryotes an
62                                              Peptide deformylase (PDF) is involved in bacterial prote
63 mple is actinonin, an inhibitor of bacterial peptide deformylase (PDF) whose activity is dependent on
64 e presumable promoter region of the gene for peptide deformylase (PDF), a metal-dependent enzyme that
65 the N-terminal Met residue of the peptide by peptide deformylase (PDF).
66                                              Peptide deformylase proteins (PDFs) participate in the N
67             Removal of the formyl group by a peptide deformylase renders the dipeptide product, which
68 modium falciparum, a complete picture of the peptide deformylase structure and function relationship
69 er in their protein biosynthetic mechanisms, peptide deformylase, the bacterial enzyme responsible fo
70 he design of effective antibiotics targeting peptide deformylase, the structures of the protein-inhib
71    Indeed, three sample mononuclear enzymes, peptide deformylase, threonine dehydrogenase, and cytosi
72 he assessment of the catalytic properties of peptide deformylase using a series of synthetic N-formyl
73   A macrocyclic, peptidomimetic inhibitor of peptide deformylase was designed by covalently cross-lin
74 porter protein expressed in a strain lacking peptide deformylase was shown to retain the formyl group