Isochorismate synthase
isochorismate synthase | |||||||||
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Identifiers | |||||||||
EC number | 5.4.4.2 | ||||||||
CAS number | 37318-53-9 | ||||||||
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 | ||||||||
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In enzymology, an isochorismate synthase (EC 5.4.4.2) is an enzyme that catalyzes the chemical reaction
- chorismate isochorismate
Hence, this enzyme has one substrate, chorismate, and one product, isochorismate.
This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring hydroxy groups. The systematic name of this enzyme class is isochorismate hydroxymutase. This enzyme participates in 2 metabolic pathways: ubiquinone biosynthesis and biosynthesis of siderophore group. In the model plant Arabidopsis thaliana, isochorismate synthase is required for salicylic acid synthesis, which occurs mainly through the chorismate-isochorismate pathway (see Wildermuth 2006 for details).
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2EUA.
References
- Young IG, Gibson F (1969). "Regulation of the enzymes involved in the biosynthesis of 2,3-dihydroxybenzoic acid in Aerobacter aerogenes and Escherichia coli". Biochim. Biophys. Acta. 177 (3): 401–11. PMID 4306838.
- van Tegelen LJ, Moreno PR, Croes AF, Verpoorte R, Wullems GJ (1999). "Purification and cDNA cloning of isochorismate synthase from elicited cell cultures of Catharanthus roseus". Plant. Physiol. 119 (2): 705–12. doi:10.1104/pp.119.2.705. PMC 32148. PMID 9952467.
- Dahm C, Muller R, Schulte G, Schmidt K, Leistner E (1998). "The role of isochorismate hydroxymutase genes entC and menF in enterobactin and menaquinone biosynthesis in Escherichia coli". Biochim. Biophys. Acta. 1425 (2): 377–86. PMID 9795253.