prephenate dehydratase

{{infobox enzyme

| Name = prephenate dehydratase

| EC_number = 4.2.1.51

| CAS_number = 9044-88-6

| GO_code = 0004664

| image = 3mwb.jpg

| width = 270

| caption = Prephenate dehydratase homotetramer, Paenarthrobacter aurescens

}}

The enzyme prephenate dehydratase ({{EnzExplorer|4.2.1.51}}) catalyzes the chemical reaction

:prephenate $\rightleftharpoons$ phenylpyruvate + H₂O + CO₂

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 prephenate hydro-lyase (decarboxylating; phenylpyruvate-forming). This enzyme is also called prephenate hydro-lyase (decarboxylating). This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis.

Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code {{PDB link|2QMX}}.

References

{{cite journal | vauthors = CERUTTI P, GUROFF G | title = Enzymatic Formation of Phenylpyruvic Acid in Pseudomonas Sp. (Atcc 11299A) and ITS Regulation | date = 1965 | journal = J. Biol. Chem. | volume = 240 | issue = 7 | pages = 3034–8 | doi = 10.1016/S0021-9258(18)97282-0 | doi-access = free | pmid = 14342329 }}
{{cite journal | vauthors = COTTON RG, GIBSON F | title = The biosynthesis of phenylalanine and tyrosine; enzymes converting chorismic acid into prephenic acid and their relationships to prephenate dehydratase and prephenate dehydrogenase | date = 1965 | journal = Biochim. Biophys. Acta | volume = 100 | pages = 76–88 | pmid = 14323651 | doi=10.1016/0304-4165(65)90429-0}}
{{cite journal |author1 = Schmidt JC |author2 =Zalkin H | date = 1969 | title = Chorismate mutase-prephenate dehydratase. Partial purification and properties of the enzyme from Salmonella typhimurium | journal = Biochemistry | volume = 8 | pages = 174–181 | doi = 10.1021/bi00829a025 | pmid=4887851 | issue = 1}}

Category:EC 4.2.1

Category:Enzymes of known structure