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Literature summary extracted from

  • Hennig, M.; Sterner, R.; Kirschner, K.; Jansonius, J.N.
    Crystal structure at 2.0 A resolution of phosphoribosyl anthranilate isomerase from the hyperthermophile Thermotoga maritima: possible determinants of protein stability (1997), Biochemistry, 36, 6009-6016.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.3.1.24 trpF gene is cloned and expressed in Escherichia coli Thermotoga maritima

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.3.1.24 x-ray structure 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 pH 7.5, 25°C, dimer Thermotoga maritima

Organism

EC Number Organism UniProt Comment Textmining
5.3.1.24 Thermotoga maritima Q56320 monofunctional enzyme
-
5.3.1.24 Thermotoga maritima Q56320 Protein Data Bank: 1NSJ
-

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 enzyme structure Thermotoga maritima 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
 ?
5.3.1.24 N-(5-phospho-beta-D-ribosyl)anthranilate high catalytic efficiency Thermotoga maritima 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
5.3.1.24 homodimer 2 identical (betaalpha)8-barrel subunits, which are associated back-to-back and locked together by a hydrophobic loop Thermotoga maritima

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
5.3.1.24 additional information
-
 structural features resonsible for the high thermostability Thermotoga maritima