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Literature summary for 3.5.1.88 extracted from

  • Groche, D.; Becker, A.; Schlichting, I.; Kabsch, W.; Schultz, S.; Wagner, A.F.V.
    Isolation and crystallization of functionally competent Escherichia coli peptide deformylase forms containing either iron or nickel in the active site (1998), Biochem. Biophys. Res. Commun., 246, 342-346.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
Fe2+-, Ni2+- and Zn2+-bound forms, hanging and sitting drop vapour diffusion techniques Escherichia coli

General Stability

General Stability Organism
Ni2+-bound enzyme fully stable, additional stabilization during purification by catalase Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
EDTA convertion to the apoenzyme during 1 h at 10 mM Escherichia coli
Zn2+ tightly bound, very poor activity Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
15
-
N-formyl-Met-Ala
-
Escherichia coli
19
-
N-formyl-Met-Ala Fe2+-bound enzyme 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
Ni2+ gives insensitivity to oxidation Escherichia coli
Zn2+ Zn2+-bound enzyme inactive in crystallization analysis Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
19000
-
gel filtration Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Oxidation Stability

Oxidation Stability Organism
sensitive to intracellular reactive oxygen Escherichia coli

Purification (Commentary)

Purification (Comment) Organism
to homogeneity, recombinant Ni2+, Fe2+- and Zn2+-bound preparations Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1200
-
Fe2+- and Ni2+-bound enzyme Escherichia coli

Storage Stability

Storage Stability Organism
4°C, 2 mg Ni2+-bound enzyme/ml, pH 7.7, several weeks Escherichia coli

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
monomer 1 * 19000, SDS-PAGE Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2100
-
N-formyl-Met-Ala recombinant Fe2+-bound enzyme Escherichia coli