Indole-3-glycerol-phosphate synthase explained

indole-3-glycerol-phosphate synthase
Ec Number:4.1.1.48
Cas Number:9031-60-1
Go Code:0004425
Width:270
Symbol:IGPS
Indole-3-glycerol phosphate synthase
Pfam:PF00218
Pfam Clan:CL0036
Interpro:IPR013798
Prosite:PDOC00536
Scop:1pii

The enzyme indole-3-glycerol-phosphate synthase (IGPS) catalyzes the chemical reaction

1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate

\rightleftharpoons

1-C-(indol-3-yl)-glycerol 3-phosphate + CO2 + H2O

This enzyme belongs to the family of lyases, to be specific, the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate carboxy-lyase [cyclizing 1-C-(indol-3-yl)glycerol-3-phosphate-forming]. Other names in common use include indoleglycerol phosphate synthetase, indoleglycerol phosphate synthase, indole-3-glycerophosphate synthase, 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate, and carboxy-lyase (cyclizing). This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis and two-component system - general. It employs one cofactor, pyruvate.

Structural studies

In some bacteria, IGPS is a single chain enzyme. In others, such as Escherichia coli, it is the N-terminal domain of a bifunctional enzyme that also catalyses N-(5'-phosphoribosyl)anthranilate isomerase (PRAI) activity, the third step of tryptophan biosynthesis. In fungi, IGPS is the central domain of a trifunctional enzyme that contains a PRAI C-terminal domain and a glutamine amidotransferase (GATase) N-terminal domain.

A structure of the IGPS domain of the bifunctional enzyme from the mesophilic bacterium E. coli (eIGPS) has been compared with the monomeric indole-3-glycerol phosphate synthase from the hyperthermophilic archaeon Sulfolobus solfataricus (sIGPS). Both are single-domain (beta/alpha)8 barrel proteins, with one (eIGPS) or two (sIGPS) additional helices inserted before the first beta strand.[1]

As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes,,,,,,,,,, and .

Further reading

Notes and References

  1. Goldman A . How to make my blood boil . Structure . 3 . 12 . 1277–9 . December 1995 . 8747452 . 10.1016/s0969-2126(01)00263-5. free .