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Literature summary for 2.4.2.18 extracted from

  • Egan, A.F.; Gibson, F.
    Anthranilate synthase-anthranilate 5-phosphoribosyl 1-pyrophosphate phosphoribosyltransferase from Aerobacter aerogenes (1972), Biochem. J., 130, 847-859.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.4.2.18

General Stability

General Stability Organism
dilution inactivates Klebsiella aerogenes
freezing and thawing inactivates Klebsiella aerogenes

Inhibitors

Inhibitors Comment Organism Structure
L-tryptophan
-
 Escherichia coli
L-tryptophan when phosphoribosyltransferase is not an aggregate with anthranilate synthase, it is not subject to tryptophan inhibition, inhibitor site is on the anthranilate synthase component Klebsiella aerogenes

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Klebsiella aerogenes

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
90000
-
 tryptophan auxotroph with no anthranilate synthase activity, sucrose density gradient sedimentation Klebsiella aerogenes
170000
-
 sucrose density gradient sedimentation, complex with anthranilate synthase activity Klebsiella aerogenes

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate Escherichia coli enzyme of tryptophan biosynthesis N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
 ?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate Klebsiella aerogenes enzyme of tryptophan biosynthesis N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 K-12
-
Klebsiella aerogenes
-
-
-

Purification (Commentary)

Purification (Comment) Organism
partial, enzyme complex Klebsiella aerogenes

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
734
-
-
 Klebsiella aerogenes

Storage Stability

Storage Stability Organism
-15°C, crude extract is stable for 2 years Klebsiella aerogenes
4°C, 10% loss of activity after 2 months Klebsiella aerogenes

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
-
 Escherichia coli N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
 ?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
-
 Klebsiella aerogenes N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
 ?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate enzyme of tryptophan biosynthesis Escherichia coli N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
 ?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate enzyme of tryptophan biosynthesis Klebsiella aerogenes N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
 ?

Subunits

Subunits Comment Organism
More in some organisms, this enzyme is part of a multifunctional protein together with one or more other components of the system for biosynthesis of tryptophan: EC 4.1.1.48, EC 4.1.3.27, EC 4.2.1.20, EC 5.3.1.24 Klebsiella aerogenes
More anthranilate synthase-phosphoribosylanthranilate transferase complex exists in Citrobacter species in all other bacteria examined phosphoribosylanthranilate transferase and anthranilate synthase are separate enzyme molecules Escherichia coli
More anthranilate synthase-phosphoribosylanthranilate transferase complex exists in Citrobacter species in all other bacteria examined phosphoribosylanthranilate transferase and anthranilate synthase are separate enzyme molecules Klebsiella aerogenes

Synonyms

Synonyms Comment Organism
More in some organisms, this enzyme is part of a multifunctional protein together with one or more other components of the system for biosynthesis of tryptophan (EC 4.1.1.48, EC 4.1.3.27, EC 4.2.1.20, EC 5.3.1.24) Klebsiella aerogenes