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Literature summary for 3.5.1.88 extracted from

  • Rajagopalan, P.T.R.; Yu, X.C.; Pei, D.
    Peptide deformylase: A new type of mononuclear iron protein (1997), J. Am. Chem. Soc., 119, 12418-12419.
No PubMed abstract available
Search for more literature for 3.5.1.88

General Stability

General Stability Organism
denaturation with guanidinium hydrochloride, protein 1 unfolds at more than 3 M, protein 2 unfolds at 1.7 M Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Fe enzyme contains iron Haemophilus influenzae
Fe enzyme form 2 contains up to 1.0 iron atom per polypeptide - 0.77 Fe2+ and 0.2 Fe3+ per polypeptide. The iron is likely coordinated by His132, His136 and Cys90 in the protein Escherichia coli
Zn2+ enzyme form 1 contains approximately 1.0 Zn2+ per polypeptide chain, the zinc-containing protein 1 is likely formed during iron depletion caused by overexpression Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
19000
-
 1 * 19000, SDS-PAGE Escherichia coli
19200
-
 1 * 19200, electrospray ionization mass spectrometry Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Haemophilus influenzae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-formyl-Met-Ala-Ser + H2O
-
 Escherichia coli formate + Met-Ala-Ser
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 19000, SDS-PAGE Escherichia coli
monomer 1 * 19200, electrospray ionization mass spectrometry Escherichia coli

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
23
-
 t1/2 is 1 min, enzyme form 2 Escherichia coli