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Literature summary extracted from

  • Walker, M.S.; DeMoss, J.A.
    Organisation of the functional domains of anthranilate synthase from Neurospora crassa (1986), J. Biol. Chem., 261, 16073-16077.
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
5.3.1.24 56000
-
 indole-3-glycerol-phosphate synthetase/PRA isomerase fragment of the multifunctional anthranilate synthetase complex beta subunit, gel filtration Neurospora crassa

Organism

EC Number Organism UniProt Comment Textmining
5.3.1.24 Neurospora crassa
-
 a fragment of the beta subunit of the multifunctional alpha2beta2 anthranilate synthetase complex has PRA isomerase and indole-3-glycerol phosphate synthetase activities, organization of the functional domains of the compex
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.3.1.24 indole-3-glycerol-phosphate synthetase/PRA isomerase fragment of the multifunctional anthranilate synthetase complex beta subunit Neurospora crassa

Source Tissue

EC Number Source Tissue Comment Organism Textmining
5.3.1.24 mycelium
-
 Neurospora crassa
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.3.1.24 N-(5-phospho-beta-D-ribosyl)anthranilate
-
 Neurospora crassa 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
5.3.1.24 dimer the indole-3-glycerol-phosphate synthetase/PRA isomerase fragment of the multifunctional anthranilate synthetase complex beta subunit exists as a dimer Neurospora crassa