Chorismate synthase

Chorismate synthase
Ribbon diagram of the 1ZTB structure.
Ribbon diagram of the 1ZTB structure, Chorismate synthase isolated from Mycobacterium tuberculosis. [1]
chorismate synthase
Identifiers
EC number 4.2.3.5
CAS number 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 / EGO

In enzymology, a chorismate synthase (EC 4.2.3.5) is an enzyme that catalyzes the chemical reaction

5-O-(1-carboxyvinyl)-3-phosphoshikimate \rightleftharpoons chorismate + phosphate

Hence, this enzyme has one substrate, 5-O-(1-carboxyvinyl)-3-phosphoshikimate, and two products, chorismate and 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
SCOP 1q1l

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.

Structural studies

As of late 2007, 9 structures have been solved for this class of enzymes, with PDB accession codes 1Q1L, 1QXO, 1R52, 1R53, 1SQ1, 1UM0, 1UMF, 1ZTB, and 2G85.

References

  1. ^ 1ZTB Dias; et al. (2006). "Structure of chorismate synthase from Mycobacterium tuberculosis". J. Structural Biology 154: 130–143. ; rendered with PyMOL
  2. ^ 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. PMID 1718979. 
  3. ^ 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. 
  • Gaertner FH, Cole KW (1973). "Properties of chorismate synthase in Neurospora crassa". J. Biol. Chem. 248 (13): 4602–9. PMID 4146266. 
  • Morell H, Clark MJ, Knowles PF, Sprinson DB (1967). "The enzymic synthesis of chorismic and prephenic acids from 3-enolpyruvylshikimic acid 5-phosphate". J. Biol. Chem. 242 (1): 82–90. PMID 4289188. 
  • Welch GR, Cole KW, Gaertner FH (1974). "Chorismate synthase of Neurospora crassa: a flavoprotein". Arch. Biochem. Biophys. 165 (2): 505–18. doi:10.1016/0003-9861(74)90276-8. PMID 4155270. 
  • Bornemann S, Lowe DJ, Thorneley RN (1996). "The transient kinetics of Escherichia coli chorismate synthase: substrate consumption, product formation, phosphate dissociation, and characterization of a flavin intermediate". Biochemistry. 35 (30): 9907–16. doi:10.1021/bi952958q. PMID 8703965. 
  • Bornemann S, Theoclitou ME, Brune M, Webb MR, Thorneley RN, Abell C (2000). "A Secondary beta Deuterium Kinetic Isotope Effect in the Chorismate Synthase Reaction". Bio-Organic. Chemistry. 28 (4): 191–204. doi:10.1006/bioo.2000.1174. PMID 11034781. 
  • Osborne A, Thorneley RN, Abell C, Bornemann S (2000). "Studies with substrate and cofactor analogues provide evidence for a radical mechanism in the chorismate synthase reaction". J. Biol. Chem. 275 (46): 35825–30. doi:10.1074/jbc.M005796200. PMID 10956653. 
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