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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

Reaction

1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
=
1-C-(indol-3-yl)glycerol 3-phosphate
+
CO2
+
H2O

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

     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.48 indole-3-glycerol-phosphate synthase

General Stability

General Stability on EC 4.1.1.48 - indole-3-glycerol-phosphate synthase

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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
guanidinium-induced denaturation. Unfolding mechanism closely approaches a two-state model at pH 7.0 and a more complex mechanism at pH 9.0
-
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)
-
optimal stabilization by 0.8 M sucrose
-
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)
-
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