Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

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

Crystallization

Crystallization on EC 4.1.1.48 - indole-3-glycerol-phosphate synthase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal packing seems to be influenced by ionic strength of the solvent
-
in complex with substrate 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate, with a substrate analogue, and with product indole-3-glycerol phosphate
molecular dynamics simulations of wild-type at 25°C in the apo form and in the presence of the substrate
mutagenesis data and crystal structure analysis of IGPS from Sulfolobus solfataricus allows for the formulation of a plausible chemical mechanism of the reaction
N-terminal deletion mutant lacking 26 amino acids, structure of core is unchanged compared to wild-type
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
contains 17 strong salt bridges
-