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Literature summary for 5.3.1.24 extracted from

  • Akanuma, S.; Yamagishi, A.
    Experimental evidence for the existence of a stable half-barrel subdomain in the (beta/alpha)8-barrel fold (2008), J. Mol. Biol., 382, 458-466.
    View publication on PubMed

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
23100
-
calculated from amino acid sequence Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli M15
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA column chromatography, HiTrap Q column chromatography, Superdex 200 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
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
-
Escherichia coli M15 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
?

Subunits

Subunits Comment Organism
dimer
-
Escherichia coli

Synonyms

Synonyms Comment Organism
N-(5'-phosphoribosyl)anthranilate isomerase
-
Escherichia coli
TrpF a (beta/alpha)8-barrel enzyme involved in the tryptophan biosynthetic pathway Escherichia coli

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
48 50 the melting temperatures of wild type TrpF are 48 and 50°C when the protein concentrations are 0.002 and 0.02 mM, respectively Escherichia coli