4.1.1.48: indole-3-glycerol-phosphate synthase
This is an abbreviated version!
For detailed information about indole-3-glycerol-phosphate synthase, go to the full flat file.
Word Map on EC 4.1.1.48
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4.1.1.48
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sulfolobus
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solfataricus
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amidotransferase
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chorismate
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prfar
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n-5'-phosphoribosylanthranilate
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on-pathway
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glutamine-dependent
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betaalpha8-barrel
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betaalpha8
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medicine
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drug development
- 4.1.1.48
- sulfolobus
- solfataricus
-
amidotransferase
- chorismate
-
prfar
-
n-5'-phosphoribosylanthranilate
-
on-pathway
-
glutamine-dependent
-
betaalpha8-barrel
-
betaalpha8
- medicine
- drug development
Reaction
Synonyms
eIGPS, IGP synthase, IGPS, indole-3-glycerol phosphate synthase, Indole-3-glycerol phosphate synthetase, Indole-3-glycerol-phosphate synthase, indole-3-glycerolphosphate synthase, Indole-3-glycerophosphate synthase, Indoleglycerol phosphate synthase, Indoleglycerol phosphate synthetase, Indoleglycerolphosphate synthetase, InGP synthase, InGP synthetase, InGPS, mIGPS, MtIGPS, Phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase, Pk-trpC, PRAI, PRAI-InGPS, sIGPS, SSO0895, Synthase, indole-3-glycerol phosphate, TrpC
ECTree
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Temperature Stability
Temperature Stability on EC 4.1.1.48 - indole-3-glycerol-phosphate synthase
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40 - 50
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little loss of activity after a 10 min heating in a water bath at temperatures from 40 to 50°C
75
80
85.5
86.5
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in 0.05 M potassium phosphate at pH 7.5. Half-life of wild-type enzyme: 46 min, half-life of mutant enzyme P2S: 18 min, hal-life of mutant enzyme F246S 1 min, half-life of mutant enzyme G212E: 38 min, half-life of mutant enzyme P2S/F246S: less than 0.1 min, half-life of mutant enzyme P2S/G212E: 19 min
90
additional information
75
half-life of wild-type, 123 min, half-life of N-terminal deletion mutant lacking 26 amino acids, 2.9 min
75
half-life of wild-type, 258 min, half-life of N-terminal deletion mutant lacking 25 amino acids, 6.3 min
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first-order kinetic constant at pH 6.5, pH 8.0 and pH 9.5: 0.020 per min
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14.4 min, half-life for irreversible thermal inactivation, mutant R241A
85.5
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36.1 min, half-life for irreversible thermal inactivation, mutant D184A
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mutant enzyme N90A shows 2fold decrease in the rate of thermal inactivation at 90°C as compared to wild-type enzyme. Thermal inactivation constant of muta t enzymes N90A or N90Q at 90°C is similar to wild-type enzyme
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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
additional information
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melting temperature is higher at alkaline that at neutral pH
additional information
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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
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