Prephenate dehydratase

From Wikipedia, the free encyclopedia

In enzymology, a prephenate dehydratase (EC 4.2.1.51) is an enzyme that catalyzes the chemical reaction

prephenate $\rightleftharpoons$ phenylpyruvate + H₂O + CO₂

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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

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

[edit] References

IUBMB entry for 4.2.1.51
BRENDA references for 4.2.1.51 (Recommended.)
PubMed references for 4.2.1.51
PubMed Central references for 4.2.1.51
Google Scholar references for 4.2.1.51
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. PMID 14323651.
Schmidt JC and Zalkin H (1969). "Chorismate mutase-prephenate dehydratase. Partial purification and properties of the enzyme from Salmonella typhimurium". Biochemistry 8: 174–181. doi:10.1021/bi00829a025.