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Literature summary for 3.5.1.88 extracted from

  • Becker, A.; Schlichting, I.; Kabsch, W.; Schultz, S.; Volker Wagner, A.F.
    Structure of peptide deformylase and identification of the substrate binding site (1998), J. Biol. Chem., 273, 11413-11416.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
structure of the catalytically active enzyme in the nickel-bound form at 2.5-A resolution and at 1.9-A resolution in complex with the competitive inhibitor polyethylene glycol molecule Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
Polyethylene glycol
-
Escherichia coli
polylethylene glycol competitive inhibitor with respect to formylmethionine Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1
-
N-formyl-Met
-
Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ enzyme contains Fe2+ Escherichia coli
Ni2+ enzyme nearly retains its activity on substitution of the naturally occuring Fe2+ by Ni2+ Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
N-formyl-L-methionine-polypeptide + H2O Escherichia coli the enzyme is requiredfor the removal of the formyl group at the N-terminus of nascent polypeptide chains formate + L-methionine-polypeptide
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-formyl-L-methionine-polypeptide + H2O the enzyme is requiredfor the removal of the formyl group at the N-terminus of nascent polypeptide chains Escherichia coli formate + L-methionine-polypeptide
-
?
N-formyl-Met + H2O
-
Escherichia coli formate + Met
-
?

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
6
-
Polyethylene glycol
-
Escherichia coli