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Literature summary extracted from

  • Hommel, U.; Lustig, A.; Kirschner, K.
    Purification and characterization of yeast anthranilate phosphoribosyltransferase (1989), Eur. J. Biochem., 180, 33-40.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.3.1.24 additional information chemically synthesized N-(5-phospho-beta-D-ribosyl)anthranilate contains inhibitors, but not if it is generated by anthranilate phosphoribosyltransferase Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.2.18 0.0016
-
anthranilate
-
Saccharomyces cerevisiae
2.4.2.18 0.0224
-
5-phospho-alpha-D-ribose 1-diphosphate
-
Saccharomyces cerevisiae
5.3.1.24 additional information
-
additional information increasing the pH from 7.5 to 8.6 increases the Km Escherichia coli
5.3.1.24 0.0049
-
N-(5-phospho-beta-D-ribosyl)anthranilate pH 7.5 Escherichia coli
5.3.1.24 0.0049
-
N-(5-phospho-beta-D-ribosyl)anthranilate 25°C, bifunctional IGPS:PRAI Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.4.2.18 Mg2+ dependent on Saccharomyces cerevisiae

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.4.2.18 42000
-
2 * 42000, SDS-PAGE Saccharomyces cerevisiae
2.4.2.18 83000
-
sedimentation equilibrium Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.2.18 anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate Saccharomyces cerevisiae enzyme of tryptophan biosynthesis N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
?
5.3.1.24 N-(5-phospho-beta-D-ribosyl)anthranilate Escherichia coli involved in tryptophan biosynthesis from chorismate 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
?
5.3.1.24 N-(5-phospho-beta-D-ribosyl)anthranilate Saccharomyces cerevisiae involved in tryptophan biosynthesis from chorismate 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.4.2.18 Saccharomyces cerevisiae
-
-
-
5.3.1.24 Escherichia coli
-
bifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex
-
5.3.1.24 Saccharomyces cerevisiae
-
naturally monofunctional enzyme
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.2.18 95% pure Saccharomyces cerevisiae
5.3.1.24
-
Saccharomyces cerevisiae
5.3.1.24 indole-3-glycerol-phosphate synthetase/PRA isomerase complex Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.4.2.18 1.58
-
-
Saccharomyces cerevisiae

Storage Stability

EC Number Storage Stability Organism
2.4.2.18 addition of 10% glycerol at -70°C and then dropping the solution into liquid N2, can be thawed and frozen several times without loss of activity Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.2.18 anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
-
Saccharomyces cerevisiae N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
?
2.4.2.18 anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate enzyme of tryptophan biosynthesis Saccharomyces cerevisiae N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
?
5.3.1.24 N-(5-phospho-beta-D-ribosyl)anthranilate
-
Escherichia coli 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
?
5.3.1.24 N-(5-phospho-beta-D-ribosyl)anthranilate
-
Saccharomyces cerevisiae 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
?
5.3.1.24 N-(5-phospho-beta-D-ribosyl)anthranilate involved in tryptophan biosynthesis from chorismate Escherichia coli 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
?
5.3.1.24 N-(5-phospho-beta-D-ribosyl)anthranilate involved in tryptophan biosynthesis from chorismate Saccharomyces cerevisiae 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
?

Subunits

EC Number Subunits Comment Organism
2.4.2.18 dimer 2 * 42000, SDS-PAGE Saccharomyces cerevisiae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.2.18 25
-
assay at Saccharomyces cerevisiae
5.3.1.24 25
-
assay at Escherichia coli
5.3.1.24 25
-
assay at Saccharomyces cerevisiae

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.4.2.18 4
-
loss of 10% activity in 24 h Saccharomyces cerevisiae

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.4.2.18 2.9
-
anthranilate cosubstrate: 5-phospho-alpha-D-ribose 1-diphosphate Saccharomyces cerevisiae
5.3.1.24 40
-
N-(5-phospho-beta-D-ribosyl)anthranilate bifunctional IGPS:PRAI Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.2.18 7.5
-
assay at Saccharomyces cerevisiae
5.3.1.24 7.5
-
assay at Escherichia coli
5.3.1.24 7.5
-
assay at Saccharomyces cerevisiae