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Literature summary extracted from

  • Sah-Teli, S.; Hynönen, M.; Sulu, R.; Dalwani, S.; Schmitz, W.; Wierenga, R.; Venkatesan, R.
    Insights into the stability and substrate specificity of the E. coli aerobic beta-oxidation trifunctional enzyme complex (2020), J. Struct. Biol., 210, 107494 .
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.1.16 modeling of the heterotetrameric alpha2beta2 complex Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.1.16 75000
-
 static light scattering Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.16 Escherichia coli P21151
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.16 acetoacetyl-CoA + CoA
-
 Escherichia coli 2 acetyl-CoA
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.1.16 dimer 2 * 42000, and monomer, calculated from sequence Escherichia coli
2.3.1.16 monomer 1 * 42000, and dimer, calculated from sequence Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
2.3.1.16 FadA
-
 Escherichia coli
2.3.1.16 TFE-beta subunit
-
 Escherichia coli

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.3.1.16 45
-
 melting temperature, isolated beta-subunit Escherichia coli
2.3.1.16 51
-
 melting temperature, heterotetrameric alpha2beta2 complex Escherichia coli

General Information

EC Number General Information Comment Organism
2.3.1.16 physiological function FadA is the bta-subunit of heterotetrameric TFE catalyzing the last three steps of the beta-oxidation. When expressed separately, TFE-alpha is a catalytically active monomer whereas TFE-beta is inactive. When mixed together, active TFE tetramer is reconstituted Escherichia coli