Imidazoleglycerol-phosphate dehydratase
| imidazoleglycerol-phosphate dehydratase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.2.1.19 | ||||||||
| CAS no. | 9024-35-5 | ||||||||
| 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 / QuickGO | ||||||||
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| Imidazoleglycerol-phosphate dehydratase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 crystal structure of imidazole glycerol phosphate dehydratase | |||||||||
| Identifiers | |||||||||
| Symbol | IGPD | ||||||||
| Pfam | PF00475 | ||||||||
| Pfam clan | CL0329 | ||||||||
| InterPro | IPR000807 | ||||||||
| PROSITE | PDOC00738 | ||||||||
| SCOP2 | 1rhy / SCOPe / SUPFAM | ||||||||
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In enzymology, an imidazoleglycerol-phosphate dehydratase (EC 4.2.1.19) is an enzyme that catalyzes the chemical reaction
- D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Hence, this enzyme has one substrate, D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate, and two products, 3-(imidazol-4-yl)-2-oxopropyl phosphate and H2O. This reaction is the sixth step in the biosynthesis of histidine in bacteria, fungi and plants.
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is D-erythro-1-(imidazol-4-yl)glycerol-3-phosphate hydro-lyase [3-(imidazol-4-yl)-2-oxopropyl-phosphate-forming]. Other names in common use include IGP dehydratase, and D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate hydro-lyase. This enzyme participates in histidine metabolism as it is involved in the 6th step of histidine biosynthesis as part of a nine step cyclical pathway.
IGPD is a recognised novel herbicide target as animals do not have an IGPD
There are two isoforms of IGPD; IGPD1 and IGPD2. The different isoforms are highly conserved with only 8 amino acids differing between them. These subtle differences however affect their activity but as yet it is unknown how.
In most organisms IGPD is a monofunctional protein of about 22 to 29 kD. In some bacteria such as Escherichia coli, it is the C-terminal domain of a bifunctional protein that include a histidinol-phosphatase domain.[1] In E. coli, this is the protein encoded by the hisB gene.[2]
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1RHY, 2AE8, and 2F1D.[3]
References
- ^ Carlomagno MS, Chiariotti L, Alifano P, Nappo AG, Bruni CB (October 1988). "Structure and function of the Salmonella typhimurium and Escherichia coli K-12 histidine operons". J. Mol. Biol. 203 (3): 585–606. doi:10.1016/0022-2836(88)90194-5. PMID 3062174.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Brilli, M.; Fani, R. (2004). "Molecular Evolution of hisB Genes". Journal of Molecular Evolution. 58 (2): 225–237. doi:10.1007/s00239-003-2547-x. PMID 15042344.
- ^ Glynn SE, Baker PJ, Sedelnikova SE, Davies CL, Eadsforth TC, Levy CW, Rodgers HF, Blackburn GM, Hawkes TR, Viner R, Rice DW (2005). "Structure and mechanism of imidazoleglycerol-phosphate dehydratase". Structure. 13 (12): 1809–17. doi:10.1016/j.str.2005.08.012. PMID 16338409.
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