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Literature summary for 2.7.7.3 extracted from

  • Geerlof, A.; Lewendon, A.; Shaw, W.V.
    Purification and characterization of phosphopantetheine adenylyltransferase from Escherichia coli (1999), J. Biol. Chem., 274, 27105-27111.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli JM101 Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.007
-
3'-dephospho-CoA 25°C, pH 8 Escherichia coli
0.022
-
diphosphate 25°C, pH 8 Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
17800
-
alpha6, 6 * 17800, SDS-PAGE Escherichia coli
71000
-
gel filtration Escherichia coli
108000
-
ultracentrifugation Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
wild-type and recombinant enzyme to homogenity Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
9.1
-
recombinant enzyme Escherichia coli
22.3
-
wild-type enzyme Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + pantetheine 4'-phosphate
-
Escherichia coli diphosphate + 3'-dephospho-CoA
-
r

Subunits

Subunits Comment Organism
hexamer alpha6, 6 * 17800, SDS-PAGE Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.000917
-
3'-dephospho-CoA 25°C, pH 8 Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.9
-
-
Escherichia coli