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Escherichia coli K-12 substr. MG1655 Reaction: 4.2.1.51

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 4.2.1.51

Enzymes and Genes:
chorismate mutase / prephenate dehydratase Inferred from experiment : pheA

In Pathway: L-phenylalanine biosynthesis I

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

Enzyme Commission Primary Name: prephenate dehydratase

Enzyme Commission Synonyms: prephenate hydro-lyase (decarboxylating)

Summary:
This is the second reaction after chorismate in the biosynthesis of phenylalanine. It differs from the corresponding step in the biosynthesis of tyrosine in that it is a dehydratase, not a dehydrogenase.

Enzyme Commission Summary:
This enzyme in the enteric bacteria also possesses chorismate mutase (EC 5.4.99.5) activity, and converts chorismate into prephenate.

Citations: [Cotton65, Cerutti65]

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Relationship Links: BRENDA:EC:4.2.1.51 , ENZYME:EC:4.2.1.51 , IUBMB-ExplorEnz:EC:4.2.1.51


References

Cerutti65: 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

Cotton65: 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


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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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