Indole-3-glycerol phosphate synthase

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<StructureSection load='' size='350' side='right' caption='Structure of IGPS complex with IGP (PDB entry [[1a53]])' scene='57/572309/Cv/1'>
<StructureSection load='' size='350' side='right' caption='Structure of IGPS complex with IGP (PDB entry [[1a53]])' scene='57/572309/Cv/1'>
== Function ==
== Function ==
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'''Indole-3-glycerol phosphate synthase''' (IGPS) catalyzes the reversible transformation of 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate (CDRP) to 1-C-(indol-e-yl)-glycerol 3-phosphate (IGP), CO2 and H2O. IGPS is part of the tryptophan biosynthesis<ref>PMID:5332729</ref>.
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'''Indole-3-glycerol phosphate synthase''' or '''imidazole glycerol phosphate synthase''' (IGPS) catalyzes the reversible transformation of 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate (CDRP) to 1-C-(indol-e-yl)-glycerol 3-phosphate (IGP), CO2 and H2O. IGPS is part of the tryptophan biosynthesis<ref>PMID:5332729</ref>.
== Structural highlights ==
== Structural highlights ==

Revision as of 10:23, 23 August 2020

Structure of IGPS complex with IGP (PDB entry 1a53)

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3D structures of IGPS

Updated on 23-August-2020

References

  1. Creighton TE, Yanofsky C. Indole-3-glycerol phosphate synthetase of Escherichia coli, an enzyme of the tryptophan operon. J Biol Chem. 1966 Oct 25;241(20):4616-24. PMID:5332729
  2. Hennig M, Darimont BD, Jansonius JN, Kirschner K. The catalytic mechanism of indole-3-glycerol phosphate synthase: crystal structures of complexes of the enzyme from Sulfolobus solfataricus with substrate analogue, substrate, and product. J Mol Biol. 2002 Jun 7;319(3):757-66. PMID:12054868 doi:http://dx.doi.org/10.1016/S0022-2836(02)00378-9

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