Prephenate dehydratase
In enzymology, a prephenate dehydratase (EC 4.2.1.51) is an enzyme that catalyzes the chemical reaction
- prephenate phenylpyruvate + H2O + CO2
| prephenate dehydratase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| 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 | ||||||||
| |||||||||
Hence, this enzyme has one substrate, prephenate, but 3 products: phenylpyruvate, H2O, and 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.
gollark: Possibly not ones with higher mining level actually. I don't know.
gollark: Yes.
gollark: Good.
gollark: (your compiler can probably do it for you)
gollark: DOWN WITH MANUALLY INLINING!
References
- CERUTTI P, GUROFF G (1965). "ENZYMATIC FORMATION OF PHENYLPYRUVIC ACID IN PSEUDOMONAS SP. (ATCC 11299A) AND ITS REGULATION". J. Biol. Chem. 240: 3034–8. PMID 14342329.
- 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.
- 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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