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Literature summary extracted from

  • Hennig, M.; Darimont, B.; Sterner, R.; Kirschner, K.; Jansonius, J.N.
    2.0 A structure of indole-3-glycerol phosphate synthase from the hyperthermophile Sulfolobus solfataricus: possible determinants of protein stability (1995), Structure, 3, 1295-1306.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.48
-
 Saccharolobus solfataricus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.1.48 2.0 A structure Saccharolobus solfataricus
4.1.1.48 vapour diffusion method in hanging drops, the 2.0 A crystal structure is determined and compared with the known 2.0 A structure of the IGPS domain of the bifunctional enzyme from Escherichia coli. Both enzymes have only 30% sequence identity, but share high structural similarity Saccharolobus solfataricus

General Stability

EC Number General Stability Organism
4.1.1.48 the higher stability of the enzyme from Sulfolobus solfataricus compared with the enzyme from E. coli seems to be the result of several improved interactions. Including a large number of salt bridges, stabilization of alpha-helices and strengthening of both polypeptide chain termini and solvent-exposed loops Escherichia coli
4.1.1.48 the higher stability of the enzyme from Sulfolobus solfataricus compared with the enzyme from E. coli seems to be the result of several improved interactions. Including a large number of salt bridges, stabilization of alpha-helices and strengthening of both polypeptide chain termini and solvent-exposed loops Saccharolobus solfataricus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.48 0.045
-
 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate pH 7.5, 25°C Saccharolobus solfataricus
4.1.1.48 0.09
-
 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate pH 7.5, 25°C Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.1.48 28600
-
 x * 28600, SDS-PAGE Saccharolobus solfataricus

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.48 Escherichia coli
-
-
-
4.1.1.48 Saccharolobus solfataricus
-
-
-
4.1.1.48 Saccharolobus solfataricus Q06121
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.48
-
 Saccharolobus solfataricus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.48 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
 Escherichia coli 1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
-
 ?
4.1.1.48 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
 Saccharolobus solfataricus 1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
-
 ?
4.1.1.48 1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
 Escherichia coli 1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
-
 ?
4.1.1.48 1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
 Saccharolobus solfataricus 1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
4.1.1.48 ? x * 28600, SDS-PAGE Saccharolobus solfataricus

Synonyms

EC Number Synonyms Comment Organism
4.1.1.48 eIGPS
-
 Escherichia coli
4.1.1.48 indole-3-glycerol phosphate synthase
-
 Escherichia coli
4.1.1.48 indole-3-glycerol phosphate synthase
-
 Saccharolobus solfataricus
4.1.1.48 sIGPS
-
 Saccharolobus solfataricus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.1.48 25
-
 assay at Escherichia coli
4.1.1.48 25
-
 assay at Saccharolobus solfataricus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4.1.1.48 additional information
-
 the higher stability of the indole-3-glycerol phosphate synthase from Sulfolobus solfataricus compared to indole-3-glycerol phosphate synthase from Escherichia coli seems to be the result of several improved interactions. These include a larger number of salt bridges, stabilization of alpha helices and strengthening of both polypeptide chain termini and solvent-exposed loops Escherichia coli
4.1.1.48 additional information
-
 the higher stability of the indole-3-glycerol phosphate synthase from Sulfolobus solfataricus compared to indole-3-glycerol phosphate synthase from Escherichia coli seems to be the result of several improved interactions. These include a larger number of salt bridges, stabilization of alpha helices and strengthening of both polypeptide chain termini and solvent-exposed loops Saccharolobus solfataricus
4.1.1.48 44
-
 half-life: 1.8 min Escherichia coli
4.1.1.48 89
-
 half-life: 4.4 min Saccharolobus solfataricus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.1.1.48 0.033
-
 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate pH 7.5, 25°C Saccharolobus solfataricus
4.1.1.48 1.2
-
 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate pH 7.5, 25°C Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.1.48 7.5
-
 assay at Escherichia coli
4.1.1.48 7.5
-
 assay at Saccharolobus solfataricus

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
4.1.1.48 1.36
-
 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate pH 7.5, 25°C Saccharolobus solfataricus
4.1.1.48 13.3
-
 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate pH 7.5, 25°C Escherichia coli