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Literature summary for 3.5.1.88 extracted from

  • Rajagopalan, P.T.R.; Grimme, S.; Pei, D.
    Characterization of Cobalt(II)-substituted peptide deformylase: Function of the metal ion and the catalytic residue Glu-133 (2000), Biochemistry, 39, 779-790.
    View publication on PubMed
Search for more literature for 3.5.1.88

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Escherichia coli

Protein Variants

Protein Variants Comment Organism
E133A 10000000fold reduction in activity Escherichia coli
E133C mutant fails to produce soluble protein Escherichia coli
E133D modest reduction in activity, less than 10fold for most of the substrates tested Escherichia coli
E133Q mutant fails to produce soluble protein Escherichia coli

General Stability

General Stability Organism
enhanced stability by binding of Co2+ Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
(S)-2-O-(H-phosphonoxy)-L-caproyl-L-Leu-p-nitroanilide similar inhibition of Fe2+- and Co2+-bound enzyme Escherichia coli
1,10-phenanthroline similar inhibition of Fe2+- and Co2+-bound enzyme Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.018
-
 N-formyl-beta-thiaphenylalanyl-lysyl-p-nitroanilide recombinant mutant E133D Co2+-bound enzyme Escherichia coli
0.018
-
 N-formylmethionyl-Leu-p-nitroanilide recombinant Co2+-bound enzyme Escherichia coli
0.02
-
 N-formylmethionyl-Leu-p-nitroanilide recombinant Fe2+-bound enzyme Escherichia coli
0.027
-
 N-formyl-beta-thiaphenylalanyl-Lys-p-nitroanilide recombinant Fe2+-bound enzyme Escherichia coli
0.028
-
 N-formylmethionyl-Leu-p-nitroanilide recombinant mutant E133D Co2+-bound enzyme Escherichia coli
0.03
-
 N-formyl-beta-thiaphenylalanyl-Lys-p-nitroanilide recombinant Co2+-bound enzyme Escherichia coli
2.64
-
 N-formyl-Met-Leu-NH2 recombinant Fe2+-bound enzyme Escherichia coli
7.36
-
 N-formylmethionylleucyl-amide recombinant Co2+-bound enzyme Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ Co2+-bound enzyme, highly stable Escherichia coli
Fe2+ natural metal, bound to active site Escherichia coli
Fe2+ sensitive to reactive oxygen 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 Co2+-bound enzyme Escherichia coli

Storage Stability

Storage Stability Organism
4°C, or at room temperature, stable for hours to days Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
formyl-L-Met-Leu-p-nitroanilide + H2O
-
 Escherichia coli formate + Met-Leu-p-nitroanilide
-
 ?
N-formyl-beta-thiaphenylalanyl-Lys-p-nitroanilide + H2O
-
 Escherichia coli formate + beta-thiaphenylalanyl-Lys-p-nitroanilide
-
 ?
N-formyl-beta-thiaphenylalanyl-peptide + H2O
-
 Escherichia coli formate + beta-thiaphenylalanyl-peptide
-
 ?
N-formyl-Met-Leu-NH2 + H2O
-
 Escherichia coli formate + Met-Leu-NH2
-
 ?
N-formyl-Met-Leu-p-nitroanilide + H2O
-
 Escherichia coli formate + Met-Leu-p-nitroanilide
-
 ?
N-formylmethionylleucyl-amide + H2O
-
 Escherichia coli formate + methionylleucyl-amide
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.2
-
 N-formylmethionylleucyl-p-nitroanilide recombinant mutant E133D Co2+-bound enzyme Escherichia coli
19
-
 N-formyl-Met-Leu-p-nitroanilide recombinant Co2+-bound enzyme Escherichia coli
70
-
 N-formylmethionylleucyl-p-nitroanilide recombinant Fe2+-bound enzyme Escherichia coli
1280
-
 N-formyl-Met-Leu-NH2 recombinant Co2+-bound enzyme Escherichia coli
1320
-
 N-formyl-Met-Leu-NH2 recombinant Fe2+-bound enzyme Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
 mutant E133D Co2+-bound enzyme Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
6.5 11.6 optimal activity within, Fe2+- and Co2+-bound enzyme Escherichia coli
7.5 9.5 mutant E133D Co2+-bound enzyme Escherichia coli

pH Stability

pH Stability pH Stability Maximum Comment Organism
5.5
-
 loss of activity below Escherichia coli