| prephenate dehydratase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Prephenate dehydratase homotetramer, Paenarthrobacter aurescens | |||||||||
| Identifiers | |||||||||
| EC no. | 4.2.1.51 | ||||||||
| CAS no. | 9044-88-6 | ||||||||
| 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 | ||||||||
| |||||||||
The enzyme prephenate dehydratase (EC 4.2.1.51) catalyzes the chemical reaction:[1][2]
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.[3][4]
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2QMX.
References
- ^ Enzyme 4.2.1.51 at KEGG Pathway Database.
- ^ Cotton RG, Gibson F (1965). "The biosynthesis of phenylalanine and tyrosine; enzymes converting chorismic acid into prephenic acid and their relationships to prephenate dehydratase and prephenate dehydrogenase". Biochim. Biophys. Acta. 100: 76–88. doi:10.1016/0304-4165(65)90429-0. PMID 14323651.
- ^ Cerutti P, Guroff G (1965). "Enzymatic Formation of Phenylpyruvic Acid in Pseudomonas Sp. (Atcc 11299A) and ITS Regulation". J. Biol. Chem. 240 (7): 3034–8. doi:10.1016/S0021-9258(18)97282-0. PMID 14342329.
- ^ Schmidt JC; Zalkin H (1969). "Chorismate mutase-prephenate dehydratase. Partial purification and properties of the enzyme from Salmonella typhimurium". Biochemistry. 8 (1): 174–181. doi:10.1021/bi00829a025. PMID 4887851.
