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Literature summary extracted from

  • Black, P.N.; Zhang, Q.; Weimar, J.D.; DiRusso, C.C.
    Mutational analysis of a fatty acyl-coenzyme A synthetase signature motif identifies seven amino acid residues that modulate fatty acid substrate specificity (1997), J. Biol. Chem., 272, 4896-4903.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
6.2.1.3 N431A 18 site-directed mutantions within the fatty acyl-CoA synthetase structural gene fadD corresponding to the FACS signature. Only one substitution results in wild-type fatty acyl-CoA synthetase activity profiles, 10 substitutions with abolished or greatly diminished enzyme activity, and seven substitutions with altered fatty acid chain length specificity. Of these seven, five also have reduced activity compared with the wild-type enzyme Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.2.1.3 ATP + long-chain carboxylic acid + CoA Escherichia coli enzyme plays a pivotal role in cellular homeostasis, particular in lipid metabolism ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.2.1.3 Escherichia coli
-
 wild-type and mutant forms
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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 + long-chain carboxylic acid + CoA enzyme plays a pivotal role in cellular homeostasis, particular in lipid metabolism Escherichia coli ?
-
 ?
6.2.1.3 ATP + myristate + CoA
-
 Escherichia coli AMP + diphosphate + myristoyl-CoA
-
 ?
6.2.1.3 ATP + oleate + CoA
-
 Escherichia coli AMP + diphosphate + oleoyl-CoA
-
 ?