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Literature summary for 3.5.1.88 extracted from

  • Wang, Q.; Wang, J.; Cai, Z.; Xu, W.
    Prediction of the binding modes between BB-83698 and peptide deformylase from Bacillus stearothermophilus by docking and molecular dynamics simulation (2008), Biophys. Chem., 134, 178-184.
    View publication on PubMed

Application

Application Comment Organism
medicine the specific bacterial requirement for peptide deformylase in protein synthesis provides a rational basis for selectivity, making it an attractive potential drug discovery target Geobacillus stearothermophilus

Inhibitors

Inhibitors Comment Organism Structure
actinonin
-
Geobacillus stearothermophilus
BB-83698
-
Geobacillus stearothermophilus

Metals/Ions

Metals/Ions Comment Organism Structure
Ni2+
-
Geobacillus stearothermophilus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Geobacillus stearothermophilus the formyl moiety of newly synthesized peptides is removed by peptide deformylase ?
-
?

Organism

Organism UniProt Comment Textmining
Geobacillus stearothermophilus O31410
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the formyl moiety of newly synthesized peptides is removed by peptide deformylase Geobacillus stearothermophilus ?
-
?

Synonyms

Synonyms Comment Organism
peptide deformylase type I and type II Geobacillus stearothermophilus