Biology:Prephenate dehydratase
From HandWiki
| prephenate dehydratase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Prephenate dehydratase homotetramer, Paenarthrobacter aurescens | |||||||||
| Identifiers | |||||||||
| EC number | 4.2.1.51 | ||||||||
| CAS number | 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 | ||||||||
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The enzyme prephenate dehydratase (EC 4.2.1.51) catalyzes the chemical reaction
- prephenate [math]\displaystyle{ \rightleftharpoons }[/math] 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 2QMX.
References
- "Enzymatic Formation of Phenylpyruvic Acid in Pseudomonas Sp. (Atcc 11299A) and ITS Regulation". J. Biol. Chem. 240: 3034–8. 1965. PMID 14342329.
- "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. 1965. doi:10.1016/0304-4165(65)90429-0. PMID 14323651.
- 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.
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