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MetabolomicsDecreasing peptide deformylase activity is a beneficial strategy for increasing formaldehyde resistance in Methylobacterium extorquens
Formaldehyde is a highly toxic metabolite that can cause extensive damage to DNA and proteins, and strategies to mitigate formaldehyde toxicity are poorly understood. Methylotrophic bacteria, such as Methylobacterium extorquens, thrive on one-carbon compounds as sole sources of carbon and energy. Th...
2026-10-05 | MTBLS15927 | MetaboLights
ProteomicsEstablishing a MS-based assay for in vivo peptide deformylase inhibition in Bacillus subtilis
The peptide deformylase inhibitor actinonin was used to treat Bacillus subtilis 168, and the proteome was analyzed using UPLC-MSE. The goal was to identify proteins that retain N-terminal formylation of the initial methionine after actinonin treatment that could be used to establish a microplate ass...
ORGANISM(S): Bacillus subtilis subsp. subtilis str. 168 
2026-02-11 | PXD064376 | Pride
Peptide deformylase Antibiotics Proteomics N-formylation Bacillus subtilis 
UnknownBacterial peptide deformylase inhibitors induce prophages in competitors.
Not available
S-EPMC12157366 | biostudies-literature
ProteomicsLarge scale investigation of the phage Vp16 PDF activity
Prokaryotic proteins must be deformylated before the removal of their first methionine. Peptide deformylase (PDF) is indispensable and guarantees this cotranslational mechanism. Recent genome sequencing and annotation studies highlighted over 2x104 putative peptide deformylase sequences. Furthermore...
ORGANISM(S): Escherichia coli 
2017-09-25 | PXD006008 | Pride
Phage N-terminal methionine excision Virus Metalloenzyme Peptide deformylase 
GenomicsDecreasing peptide deformylase activity is a beneficial strategy for increasing formaldehyde resistance via global reprogramming in Methylobacterium extorquens
Decreasing peptide deformylase activity is a beneficial strategy for increasing formaldehyde resistance via global reprogramming in Methylobacterium extorquens
PRJNA1518879 | ENA
UnknownGeometric preferences in iron(II) and zinc(II) model complexes of peptide deformylase.
Not available
S-EPMC2760226 | biostudies-literature
UnknownThree consecutive arginines are important for the mycobacterial peptide deformylase enzyme activity.
Not available
S-EPMC3259783 | biostudies-literature
UnknownExpression, crystallization and preliminary X-ray crystallographic analysis of peptide deformylase from Campylobacter jejuni.
Not available
S-EPMC3792670 | biostudies-literature
UnknownInhibition of human peptide deformylase disrupts mitochondrial function.
Not available
S-EPMC2953058 | biostudies-literature
UnknownTotal synthesis of (±)-fumimycin and analogues for biological evaluation as peptide deformylase inhibitors.
Not available
S-EPMC6759494 | biostudies-literature
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