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Literature summary for 3.5.1.88 extracted from

  • Berg, A.K.; Srivastava, D.K.
    Delineation of alternative conformational states in Escherichia coli peptide deformylase via thermodynamic studies for the binding of actinonin (2009), Biochemistry, 48, 1584-1594.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.5.1.88

Application

Application Comment Organism
medicine peptide deformylase becomes a target for the design of new antibiotics Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
-
 Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
actinonin
-
 Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ pysiological metal ion Escherichia coli
Ni2+
-
 Escherichia coli
Zn2+
-
 Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
22000
-
 determined by SDS-PAGE Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli the removal of the formyl group from formylated methionine residues is facilitated by the action of peptide deformylase ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A6K3
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the removal of the formyl group from formylated methionine residues is facilitated by the action of peptide deformylase Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
monomer
-
 Escherichia coli

Synonyms

Synonyms Comment Organism
peptide deformylase
-
 Escherichia coli