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Literature summary extracted from

  • Kameda, K.; Imai, Y.
    Isolation and characterization of the multiple charge isoforms of acyl-CoA synthetase from Escherichia coli (1985), Biochim. Biophys. Acta, 832, 343-350.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.2.1.3 0.00017
-
 stearate acyl-CoA synthetase-4.6 Escherichia coli
6.2.1.3 0.0002
-
 myristate acyl-CoA synthetase-4.6 Escherichia coli
6.2.1.3 0.00021
-
 palmitate acyl-CoA synthetase-4.6 Escherichia coli
6.2.1.3 0.00028
-
 stearate acyl-CoA synthetase-5.6 Escherichia coli
6.2.1.3 0.00051
-
 laurate acyl-CoA synthetase-5.6 Escherichia coli
6.2.1.3 0.00072
-
 Octanoate acyl-CoA synthetase-4.6 Escherichia coli
6.2.1.3 0.0012
-
 myristate acyl-CoA synthetase-5.6 Escherichia coli
6.2.1.3 0.0019
-
 laurate acyl-CoA synthetase-4.6 Escherichia coli
6.2.1.3 0.002
-
 laurate acyl-CoA synthetase-5.0 Escherichia coli
6.2.1.3 0.0021
-
 myristate acyl-CoA synthetase-5.0 Escherichia coli
6.2.1.3 0.0029
-
 palmitate acyl-CoA synthetase-5.6 Escherichia coli
6.2.1.3 0.004
-
 Decanoate acyl-CoA synthetase-5.0 Escherichia coli
6.2.1.3 0.0059
-
 Octanoate acyl-CoA synthetase-5.6 Escherichia coli
6.2.1.3 0.0063
-
 Decanoate acyl-CoA synthetase-4.6 Escherichia coli
6.2.1.3 0.0083
-
 Decanoate acyl-CoA synthetase-5.6 Escherichia coli
6.2.1.3 0.0091
-
 stearate acyl-CoA synthetase-5.0 Escherichia coli
6.2.1.3 0.0125
-
 Octanoate acyl-CoA synthetase-5.0 Escherichia coli
6.2.1.3 0.0143
-
 palmitate acyl-CoA synthetase-5.0 Escherichia coli
6.2.1.3 0.025
-
 ATP acyl-CoA synthetase-5.6 Escherichia coli
6.2.1.3 0.033
-
 ATP acyl-CoA synthetase-5.0 Escherichia coli
6.2.1.3 0.034
-
 CoA acyl-CoA synthetase-5.6 Escherichia coli
6.2.1.3 0.035
-
 CoA acyl-CoA synthetase-5.0 Escherichia coli
6.2.1.3 0.05
-
 ATP acyl-CoA synthetase-4.6 Escherichia coli
6.2.1.3 0.053
-
 CoA acyl-CoA synthetase-4.6 Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
6.2.1.3 42000
-
 x * 42000, SDS-PAGE Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
6.2.1.3 Escherichia coli
-
 multiple charge isoforms: 4.6, 5.0 and 5.6
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
6.2.1.3 additional information enzyme does not contain carbohydrate, phospholipid and fatty acid Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.2.1.3 ATP + decanoate + CoA
-
 Escherichia coli AMP + diphosphate + decanoyl-CoA
-
 ?
6.2.1.3 ATP + laurate + CoA
-
 Escherichia coli AMP + diphosphate + lauroyl-CoA
-
 ?
6.2.1.3 ATP + myristate + CoA
-
 Escherichia coli AMP + diphosphate + myristoyl-CoA
-
 ?
6.2.1.3 ATP + octanoate + CoA
-
 Escherichia coli AMP + diphosphate + octanoyl-CoA
-
 ?
6.2.1.3 ATP + palmitate + CoA
-
 Escherichia coli AMP + diphosphate + palmitoyl-CoA
-
 ?
6.2.1.3 ATP + stearate + CoA
-
 Escherichia coli AMP + diphosphate + stearoyl-CoA
-
 ?

Subunits

EC Number Subunits Comment Organism
6.2.1.3 ? x * 42000, SDS-PAGE Escherichia coli

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
6.2.1.3 46
-
 5 min: 22% loss of acyl-CoA synthetase-4.6 activity, 38% loss of acyl-CoA synthetase-5.6 activity, 80% loss of acyl-CoA synthetase 5.0 activity Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.2.1.3 7.8 8.9 acyl-CoA synthetase-5.0 Escherichia coli
6.2.1.3 8.1
-
 acyl-CoA synthetase-4.6 and acyl-CoA synthetase-5.6. Acyl-CoA synthetase-4.6 has a second optimum at pH 8.5-9.4 Escherichia coli
6.2.1.3 8.5 9.4 acyl-CoA synthetase-4.6 has a second optimum at pH 8.1 Escherichia coli