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Literature summary extracted from

  • Moon, J.H.; Park, J.K.; Kim, E.E.
    Structure analysis of peptide deformylase from Bacillus cereus (2005), Proteins, 61, 217-220.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.5.1.88 medicine peptide deformylase has been considered as a potential target in antimicrobial chemotherapy Bacillus cereus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.5.1.88 inhibitor free structure, resolution range 50-1.7 A - peptide deformylase-actinonin complex, resolution 50-2.0 A Bacillus cereus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.1.88 actinonin
-
Bacillus cereus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.1.88 Fe2+
-
Bacillus cereus
3.5.1.88 Ni2+
-
Bacillus cereus

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 Bacillus cereus
-
formate + methionyl peptide
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.88 Bacillus cereus
-
-
-

Substrates and Products (Substrate)

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

Synonyms

EC Number Synonyms Comment Organism
3.5.1.88 BcPDF
-
Bacillus cereus
3.5.1.88 PDF
-
Bacillus cereus
3.5.1.88 peptide deformylase
-
Bacillus cereus