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Literature summary for 5.3.1.24 extracted from

  • Evran, S.; Telefoncu, A.; Sterner, R.
    Directed evolution of (betaalpha)8-barrel enzymes: establishing phosphoribosylanthranilate isomerisation activity on the scaffold of the tryptophan synthase alpha-subunit (2012), Protein Eng. Des. Sel., 25, 285-293.
    View publication on PubMed
Search for more literature for 5.3.1.24

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Thermotoga maritima

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.28
-
 N-(5-phospho-beta-D-ribosyl)anthranilate in 50 mM HEPES, pH 7.5 at 25°C Thermotoga maritima

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Thermotoga maritima
-
-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
phosphoribosylanthranilate isomerase
-
 Thermotoga maritima
PRA isomerase
-
 Thermotoga maritima
TrpF
-
 Thermotoga maritima

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.7
-
 N-(5-phospho-beta-D-ribosyl)anthranilate in 50 mM HEPES, pH 7.5 at 25°C Thermotoga maritima

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
13000
-
 N-(5-phospho-beta-D-ribosyl)anthranilate in 50 mM HEPES, pH 7.5 at 25°C Thermotoga maritima