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Literature summary for 3.5.1.88 extracted from

  • Rajagopalan, P.T.R.; Pei, D.
    Oxygen-mediated inactivation of peptide deformylase (1998), J. Biol. Chem., 273, 22305-22310.
    View publication on PubMed
Search for more literature for 3.5.1.88

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Escherichia coli

General Stability

General Stability Organism
enhanced stabilitiy in concentrated form Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
Fe3+ inactivation due to oxidation of Fe2+ to Fe3+ Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ natural metal, bound to active site Escherichia coli
Fe2+ sensitive to reactive oxygen Escherichia coli
Zn2+ Zn2+-bound form not sensitive to oxidation Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
19200
-
 gel filtration, electrospray ionization mass spectrometry Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Oxidation Stability

Oxidation Stability Organism
presence of H2O2 and O2 leads to inactivation, enzymatic exclusion of O2 renders the deformylase highly stable. Zn2+-bound enzyme form is not sensitive to oxidation Escherichia coli
sensitive to intracellular reactive oxygen Escherichia coli

Purification (Commentary)

Purification (Comment) Organism
to homogeneity, improved technique for protection to oxidation Escherichia coli

Source Tissue

Source Tissue Comment Organism Textmining
cell culture
-
 Escherichia coli
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-formyl-Met-Leu-p-nitroanilide + H2O
-
 Escherichia coli formate + Met-Leu-p-nitroanilide
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
22
-
 t1/2 is 1 min Escherichia coli