Indole-3-glycerol-phosphate synthase
| indole-3-glycerol-phosphate synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 4.1.1.48 | ||||||||
| CAS number | Template:CAS | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / EGO | ||||||||
|
|||||||||
| Indole-3-glycerol phosphate synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| File:PDB 1pii EBI.jpg
three-dimensional structure of the bifunctional enzyme phosphoribosylanthranilate isomerase: indoleglycerolphosphate synthase from escherichia coli refined at 2.0 angstroms resolution
|
|||||||||
| Identifiers | |||||||||
| Symbol | IGPS | ||||||||
| Pfam | PF00218 | ||||||||
| Pfam clan | CL0036 | ||||||||
| InterPro | IPR013798 | ||||||||
| PROSITE | PDOC00536 | ||||||||
| SCOP | 1pii | ||||||||
| SUPERFAMILY | 1pii | ||||||||
|
|||||||||
In enzymology, an indole-3-glycerol-phosphate synthase (IGPS) (EC 4.1.1.48) is an enzyme that catalyzes the chemical reaction
- 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
1-C-(indol-3-yl)-glycerol 3-phosphate + CO2 + H2O
Hence, this enzyme has one substrate, 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate, but 3 products: 1-C-(indol-3-yl)-glycerol 3-phosphate, CO2, and 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 (EC 5.3.1.24) (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 (EC 2.4.2.-) (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 1A53, 1I4N, 1J5T, 1JCM, 1JUK, 1JUL, 1LBF, 1LBL, 1PII, 1VC4, and 2C3Z.
References
<templatestyles src="Reflist/styles.css" />
Cite error: Invalid <references> tag; parameter "group" is allowed only.
<references />, or <references group="..." />Further reading
- Lua error in package.lua at line 80: module 'strict' not found.
- Lua error in package.lua at line 80: module 'strict' not found.
- Lua error in package.lua at line 80: module 'strict' not found.
This article incorporates text from the public domain Pfam and InterPro IPR013798
<templatestyles src="Asbox/styles.css"></templatestyles>
- ↑ Lua error in package.lua at line 80: module 'strict' not found.
