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Literature summary for 6.2.1.3 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
Search for more literature for 6.2.1.3

KM Value [mM]

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

Molecular Weight [Da]

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

Organism

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

Posttranslational Modification

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

Substrates and Products (Substrate)

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

Subunits

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

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
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

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8 8.9 acyl-CoA synthetase-5.0 Escherichia coli
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
8.5 9.4 acyl-CoA synthetase-4.6 has a second optimum at pH 8.1 Escherichia coli