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Literature summary for 3.5.1.88 extracted from

  • Durand, D.J.; Green, B.G.; OæConnell, J.F.; Grant, S.K.
    Peptide aldehyde inhibitors of bacterial peptide deformylase (1999), Arch. Biochem. Biophys., 367, 297-302.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
1,10-phenanthroline competitive with respect to N-formyl-Met-Val; time-dependent inhibition of cobalt-substituted enzyme with loss of the active site metal Bacillus subtilis
1,10-phenanthroline competitive with respect to N-formyl-Met-Val Escherichia coli
N-benzyloxycarbonyl-Leu-norleucinal most potent competitive inhibitor Bacillus subtilis
N-benzyloxycarbonyl-Leu-norleucinal most potent competitive inhibitor Escherichia coli
Peptide aldehydes peptide aldehydes containing a methional or leucinal Bacillus subtilis
Peptide aldehydes peptide aldehydes containing a methional or leucinal Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ cobalt-substituted enzyme Bacillus subtilis
Co2+ cobalt-substituted enzyme Escherichia coli
Zn2+ zinc metalloprotease Bacillus subtilis
Zn2+ zinc metalloprotease Escherichia coli

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-formyl-L-Met-Val + H2O
-
Bacillus subtilis formate + L-Met-Val
-
?
N-formyl-L-Met-Val + H2O
-
Escherichia coli formate + L-Met-Val
-
?

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0095
-
N-benzyloxycarbonyl-Leu-norleucinal cobalt-substituted enzyme Escherichia coli
0.0124
-
N-benzyloxycarbonyl-Leu-norleucinal cobalt-substituted enzyme Bacillus subtilis
0.026
-
N-benzyloxycarbonyl-Leu-norleucinal
-
Escherichia coli
0.0556
-
N-benzyloxycarbonyl-Leu-norleucinal
-
Bacillus subtilis