Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Howard, M.H.; Cenizal, T.; Gutteridge, S.; Hanna, W.S.; Tao, Y.; Totrov, M.; Wittenbach, V.A.; Zheng, Y.J.
    A novel class of inhibitors of peptide deformylase discovered through high-throughput screening and virtual ligand screening (2004), J. Med. Chem., 47, 6669-6672.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.5.1.88 medicine peptide deformylase is a promising antibacterial and herbicide target Glycine max

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.1.88 2-thioxo-4-thiazolidinones
-
 Glycine max
3.5.1.88 actinonin
-
 Glycine max

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.1.88 Fe2+
-
 Glycine max

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.1.88 formyl-L-methionyl peptide + H2O Glycine max
-
 formate + methionyl peptide
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.88 Glycine max
-
 3D homology model of the matured soybean PDF2 based on the X-ray structure of the homologous enzyme from Plasmodium falciparum
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.88 formyl-L-methionyl peptide + H2O
-
 Glycine max formate + methionyl peptide
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.5.1.88 PDF
-
 Glycine max
3.5.1.88 peptide deformylase
-
 Glycine max