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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Reaction
Reaction on EC 4.1.1.48 - indole-3-glycerol-phosphate synthase
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1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
in some organisms, this enzyme is part of a multifunctional protein, together with one or more other components of the system for the biosynthesis of tryptophan [2.4.2.18 (anthranilate phosphoribosyltransferase), 4.1.3.27 (anthranilate synthase), 4.2.1.20 (tryptophan synthase) and 5.3.1.24 (phosphoribosylanthranilate isomerase)]
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1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
mechanism, structures of two putative catalytic intermediates
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
molecular dynamics simulation study of the enzyme-substrate complex at room temperature and at 110°C. Relative specific activity increases 4200fold up to 110°C. Active site residues K53 and K110 control the binding of substrate in the favorable orientation for the general acid-catalyzed intramolecular ring formation reaction
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
molecular dynamics study at different temperatures. K110 is the general acid, E210 the general base. At higher temperature, the enzyme-substrate electrostatic interaction favors the binding of the substrate in near attack conformation, at lower temperature, the substrate is bound in nonreactive conformation