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Literature summary extracted from

  • Sawula, R.V.; Crawford, I.P.
    Anthranilate synthetase of Acinetobacter calcoaceticus. Separation and partial characterization of subunits (1973), J. Biol. Chem., 248, 3573-3581.
    View publication on PubMed

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.3.27 14000
-
1 * 14000 + 1 * 70000, gel filtration or sucrose density gradient centrifugation after separation of subunits Acinetobacter calcoaceticus
4.1.3.27 70000
-
1 * 14000 + 1 * 70000, gel filtration or sucrose density gradient centrifugation after separation of subunits Acinetobacter calcoaceticus
4.1.3.27 86000
-
gel filtration or sucrose density gradient centrifugation in presence of 30% glycerol Acinetobacter calcoaceticus

Organism

EC Number Organism UniProt Comment Textmining
4.1.3.27 Acinetobacter calcoaceticus
-
wild-type and 2 classes of mutants: one is defective in the chorismate-binding subunit E and is incapable of catalyzing the anthranilate synthetase reaction. The second class is defective in the G subunit but produces an active E subunit, this mutation results in a requirement for p-aminobenzoate in addition to anthranilate
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.3.27 chorismate + L-Gln
-
Acinetobacter calcoaceticus anthranilate + pyruvate + L-glutamate
-
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Subunits

EC Number Subunits Comment Organism
4.1.3.27 dimer 1 * 14000 + 1 * 70000, gel filtration or sucrose density gradient centrifugation after separation of subunits Acinetobacter calcoaceticus