| chorismate synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Chorismate synthase homotetramer, Streptococcus pneumoniae | |||||||||
| Identifiers | |||||||||
| EC no. | 4.2.3.5 | ||||||||
| CAS no. | 9077-07-0 | ||||||||
| 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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The enzyme chorismate synthase (EC 4.2.3.5) catalyzes the chemical reaction
- 5-O-(1-carboxyvinyl)-3-phosphoshikimate chorismate + phosphate
This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on phosphates. The systematic name of this enzyme class is 5-O-(1-carboxyvinyl)-3-phosphoshikimate phosphate-lyase (chorismate-forming). This enzyme is also called 5-O-(1-carboxyvinyl)-3-phosphoshikimate phosphate-lyase. This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis.
| Chorismate synthase | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||||
| Symbol | Chorismate_synt | ||||||||||
| Pfam | PF01264 | ||||||||||
| InterPro | IPR000453 | ||||||||||
| PROSITE | PDOC00628 | ||||||||||
| SCOP2 | 1q1l / SCOPe / SUPFAM | ||||||||||
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Chorismate synthase catalyzes the last of the seven steps in the shikimate pathway which is used in prokaryotes, fungi and plants for the biosynthesis of aromatic amino acids. It catalyzes the 1,4-trans elimination of the phosphate group from 5-enolpyruvylshikimate-3-phosphate (EPSP) to form chorismate which can then be used in phenylalanine, tyrosine or tryptophan biosynthesis. Chorismate synthase requires the presence of a reduced flavin mononucleotide (FMNH2 or FADH2) for its activity. Chorismate synthase from various sources shows[2][3] a high degree of sequence conservation. It is a protein of about 360 to 400 amino-acid residues.
- ^ 1ZTB Dias; et al. (2006). "Structure of chorismate synthase from Mycobacterium tuberculosis". Journal of Structural Biology. 154 (2): 130–143. doi:10.1016/j.jsb.2005.12.008. PMID 16459102.; rendered with PyMOL
- ^ Schaller A, Schmid J, Leibinger U, Amrhein N (1991). "Molecular cloning and analysis of a cDNA coding for chorismate synthase from the higher plant Corydalis sempervirens Pers". J. Biol. Chem. 266 (32): 21434–21438. doi:10.1016/S0021-9258(18)54657-3. PMID 1718979.
- ^ Braus GH, Reusser U, Jones DG (1991). "Molecular cloning, characterization and analysis of the regulation of the ARO2 gene, encoding chorismate synthase, of Saccharomyces cerevisiae". Mol. Microbiol. 5 (9): 2143–2152. doi:10.1111/j.1365-2958.1991.tb02144.x. PMID 1837329. S2CID 39999230.