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Literature summary for 3.5.1.88 extracted from

  • Gao, J.; Liang, L.; Zhu, Y.; Qiu, S.; Wang, T.; Zhang, L.
    Ligand and structure-based approaches for the identification of peptide deformylase inhibitors as antibacterial drugs (2016), Int. J. Mol. Sci., 17, E1141 .
    View publication on PubMedView publication on EuropePMC
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Application

Application Comment Organism
drug development the enzyme is an important antibacterial drug target Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
actinonin
-
 Escherichia coli
additional information ligand and structure-based approaches for identification of peptide deformylase inhibitors as antibacterial drugs, development of pharmacophore models, molecular docking using the crystal structure of Escherichia coli PDF (PDB ID 1G2A), in silico pharmacokinetic and toxicity prediction studies, overview. Computer-aided drug design (CADD) Escherichia coli
ZINC00323509
-
 Escherichia coli
ZINC03088016
-
 Escherichia coli
ZINC03984371
-
 Escherichia coli
ZINC04992698
-
 Escherichia coli
ZINC08740166
-
 Escherichia coli
ZINC12652500
-
 Escherichia coli
ZINC12658529
-
 Escherichia coli
ZINC12660672
-
 Escherichia coli
ZINC12876445
-
 Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
additional information a metalloprotease Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A6K3
-
-

Synonyms

Synonyms Comment Organism
PDF
-
 Escherichia coli

General Information

General Information Comment Organism
physiological function peptide deformylase (PDF) is a metalloprotease catalyzing the removal of a formyl group from newly synthesized proteins Escherichia coli