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Literature summary extracted from

  • Reisinger, B.; Bocola, M.; List, F.; Claren, J.; Rajendran, C.; Sterner, R.
    A sugar isomerization reaction established on various (betaalpha)8-barrel scaffolds is based on substrate-assisted catalysis (2012), Protein Eng. Des. Sel., 25, 751-760.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
5.3.1.24 D127V the mutant shows strongly reduced activity compared to the wild type enzyme Thermotoga maritima
5.3.1.24 D127V/D169V the mutant shows strongly reduced activity compared to the wild type enzyme Thermotoga maritima
5.3.1.24 D127V/D173V the mutant shows strongly reduced activity compared to the wild type enzyme Thermotoga maritima
5.3.1.24 D130V the mutant shows strongly reduced activity compared to the wild type enzyme Thermotoga maritima
5.3.1.24 D130V/D176V the mutant shows strongly reduced activity compared to the wild type enzyme Thermotoga maritima
5.3.1.24 D169V the mutant shows strongly reduced activity compared to the wild type enzyme Thermotoga maritima
5.3.1.24 D173V the mutant shows strongly reduced activity compared to the wild type enzyme Thermotoga maritima
5.3.1.24 D176V inactive Thermotoga maritima

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.3.1.24 0.00028
-
N-(5-phospho-beta-D-ribosyl)anthranilate wild type enzyme, in 50 mM HEPES, pH 7.5, at 25°C Thermotoga maritima
5.3.1.24 0.018
-
N-(5-phospho-beta-D-ribosyl)anthranilate mutant enzyme D130V/D176V, in 50 mM HEPES, pH 7.5, at 25°C Thermotoga maritima
5.3.1.24 0.019
-
N-(5-phospho-beta-D-ribosyl)anthranilate mutant enzyme D127V/D173V, in 50 mM HEPES, pH 7.5, at 25°C Thermotoga maritima
5.3.1.24 0.036
-
N-(5-phospho-beta-D-ribosyl)anthranilate mutant enzyme D127V/D169V, in 50 mM HEPES, pH 7.5, at 25°C Thermotoga maritima
5.3.1.24 0.036
-
N-(5-phospho-beta-D-ribosyl)anthranilate mutant enzyme D169V, in 50 mM HEPES, pH 7.5, at 25°C Thermotoga maritima
5.3.1.24 0.053
-
N-(5-phospho-beta-D-ribosyl)anthranilate mutant enzyme D173V, in 50 mM HEPES, pH 7.5, at 25°C Thermotoga maritima
5.3.1.24 0.074
-
N-(5-phospho-beta-D-ribosyl)anthranilate mutant enzyme D127V, in 50 mM HEPES, pH 7.5, at 25°C Thermotoga maritima
5.3.1.24 0.074
-
N-(5-phospho-beta-D-ribosyl)anthranilate mutant enzyme D130V, in 50 mM HEPES, pH 7.5, at 25°C Thermotoga maritima

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.3.1.24 N-(5-phospho-beta-D-ribosyl)anthranilate Thermotoga maritima
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
?

Organism

EC Number Organism UniProt Comment Textmining
5.3.1.24 Thermotoga maritima
-
-
-

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
-
Thermotoga maritima 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
?

Synonyms

EC Number Synonyms Comment Organism
5.3.1.24 phosphoribosylanthranilate isomerase
-
Thermotoga maritima
5.3.1.24 PRA isomerase
-
Thermotoga maritima
5.3.1.24 TrpF
-
Thermotoga maritima

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.3.1.24 0.000183
-
N-(5-phospho-beta-D-ribosyl)anthranilate mutant enzyme D130V, in 50 mM HEPES, pH 7.5, at 25°C Thermotoga maritima
5.3.1.24 0.000283
-
N-(5-phospho-beta-D-ribosyl)anthranilate mutant enzyme D173V, in 50 mM HEPES, pH 7.5, at 25°C Thermotoga maritima
5.3.1.24 0.0012
-
N-(5-phospho-beta-D-ribosyl)anthranilate mutant enzyme D130V/D176V, in 50 mM HEPES, pH 7.5, at 25°C Thermotoga maritima
5.3.1.24 0.009
-
N-(5-phospho-beta-D-ribosyl)anthranilate mutant enzyme D127V, in 50 mM HEPES, pH 7.5, at 25°C Thermotoga maritima
5.3.1.24 0.028
-
N-(5-phospho-beta-D-ribosyl)anthranilate mutant enzyme D169V, in 50 mM HEPES, pH 7.5, at 25°C Thermotoga maritima
5.3.1.24 0.032
-
N-(5-phospho-beta-D-ribosyl)anthranilate mutant enzyme D127V/D173V, in 50 mM HEPES, pH 7.5, at 25°C Thermotoga maritima
5.3.1.24 0.522
-
N-(5-phospho-beta-D-ribosyl)anthranilate mutant enzyme D127V/D169V, in 50 mM HEPES, pH 7.5, at 25°C Thermotoga maritima
5.3.1.24 3.7
-
N-(5-phospho-beta-D-ribosyl)anthranilate wild type enzyme, in 50 mM HEPES, pH 7.5, at 25°C Thermotoga maritima

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
5.3.1.24 0.018
-
N-(5-phospho-beta-D-ribosyl)anthranilate mutant enzyme D130V/D176V, in 50 mM HEPES, pH 7.5, at 25°C Thermotoga maritima
5.3.1.24 0.019
-
N-(5-phospho-beta-D-ribosyl)anthranilate mutant enzyme D127V/D173V, in 50 mM HEPES, pH 7.5, at 25°C Thermotoga maritima
5.3.1.24 0.036
-
N-(5-phospho-beta-D-ribosyl)anthranilate mutant enzyme D127V/D169V, in 50 mM HEPES, pH 7.5, at 25°C Thermotoga maritima
5.3.1.24 0.036
-
N-(5-phospho-beta-D-ribosyl)anthranilate mutant enzyme D169V, in 50 mM HEPES, pH 7.5, at 25°C Thermotoga maritima
5.3.1.24 0.053
-
N-(5-phospho-beta-D-ribosyl)anthranilate mutant enzyme D173V, in 50 mM HEPES, pH 7.5, at 25°C Thermotoga maritima
5.3.1.24 0.074
-
N-(5-phospho-beta-D-ribosyl)anthranilate mutant enzyme D127V, in 50 mM HEPES, pH 7.5, at 25°C Thermotoga maritima
5.3.1.24 0.074
-
N-(5-phospho-beta-D-ribosyl)anthranilate mutant enzyme D130V, in 50 mM HEPES, pH 7.5, at 25°C Thermotoga maritima
5.3.1.24 13000
-
N-(5-phospho-beta-D-ribosyl)anthranilate wild type enzyme, in 50 mM HEPES, pH 7.5, at 25°C Thermotoga maritima