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Prephenate dehydratase

From Wikipedia, the free encyclopedia
prephenate dehydratase
Prephenate dehydratase homotetramer, Paenarthrobacter aurescens
Identifiers
EC no.4.2.1.51
CAS no.9044-88-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

The enzyme prephenate dehydratase (EC 4.2.1.51) catalyzes the chemical reaction

prephenate 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

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

References

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  • 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.
  • 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.