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
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General Stability
General Stability on EC 4.1.1.48 - indole-3-glycerol-phosphate synthase
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guanidinium-induced denaturation. Unfolding mechanism closely approaches a two-state model at pH 7.0 and a more complex mechanism at pH 9.0
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half-life after trypsinolysis in 0.1 M Tris acetate at pH 7.8 and 25°C: wild-type enzyme (120 min), mutant enzyme P2S (60 min), mutant enzyme F246S (40 min), mutant enzyme G212E (40 min), mutant enzyme P2S/F246S (8 min), mutant enzyme P2S/G212E (15 min)
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the enzyme is strongly stabilized in phosphate buffer (t1/2: 46 min at 87°C) in comparison to HEPPS buffer (t1/2: 4.4 min at 89°C)
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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
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
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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