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Literature summary for 5.3.1.24 extracted from

  • Setiyaputra, S.; Mackay, J.P.; Patrick, W.M.
    The structure of a truncated phosphoribosylanthranilate isomerase suggests a unified model for evolution of the (betaalpha)8 barrel fold (2011), J. Mol. Biol., 408, 291-303.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
15100
-
1 * 15100, multi-angle laser light-scattering Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P00909
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA agarose column chromatography and Superdex 75 gel filtration Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-(5-phospho-beta-D-ribosyl)anthranilate
-
Escherichia coli 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
?

Subunits

Subunits Comment Organism
monomer 1 * 15100, multi-angle laser light-scattering Escherichia coli

Synonyms

Synonyms Comment Organism
N-(5'-phosphoribosyl)anthranilate isomerase
-
Escherichia coli
PRAI PRAI is the C-terminal domain of a bifunctional indole-3-glycerol phosphate synthase:N-(5'-phosphoribosyl)anthranilate isomerase enzyme in Escherichia coli Escherichia coli