In enzymology, an isochorismatase (EC 3.3.2.1) is an enzyme that catalyzes the chemical reaction
| isochorismatase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.3.2.1 | ||||||||
| CAS no. | 37288-64-5 | ||||||||
| 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 | ||||||||
| |||||||||
- isochorismate + H2O 2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate
Thus, the two substrates of this enzyme are isochorismate and H2O, whereas its two products are 2,3-dihydroxy-2,3-dihydrobenzoate and pyruvate.
This enzyme belongs to the family of hydrolases, specifically those acting on ether bonds (ether hydrolases). The systematic name of this enzyme class is isochorismate pyruvate-hydrolase. Other names in common use include 2,3-dihydro-2,3-dihydroxybenzoate synthase, 2,3-dihydroxy-2,3-dihydrobenzoate synthase, and 2,3-dihydroxy-2,3-dihydrobenzoic synthase. This enzyme participates in the biosynthesis of siderophore group (nonribosomal).
Structural studies
editAs of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1NF8, 1NF9, and 2FQ1.
References
edit- 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. doi:10.1016/0304-4165(69)90302-x. PMID 4306838.
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