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Literature summary for 4.2.1.51 extracted from

  • Liberles, J.S.; Thorolfsson, M.; Martinez, A.
    Allosteric mechanisms in ACT domain containing enzymes involved in amino acid metabolism (2005), Amino Acids, 28, 1-12.
    View publication on PubMed
Search for more literature for 4.2.1.51

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
prephenate Escherichia coli the enzyme is a bifunctional chorismate mutase/prephenate dehydratase which also possesses chorismate mutase activity, EC 5.4.99.5, and converts chorismate into prephenate, catalyzes the first to steps in the biosynthesis of L-Phe and L-Tyr phenylpyruvate + H2O + CO2
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 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
prephenate the enzyme is a bifunctional chorismate mutase/prephenate dehydratase which also possesses chorismate mutase activity, EC 5.4.99.5, and converts chorismate into prephenate, catalyzes the first to steps in the biosynthesis of L-Phe and L-Tyr Escherichia coli phenylpyruvate + H2O + CO2
-
 ?
prephenate the enzyme is a bifunctional chorismate mutase/prephenate dehydratase which also possesses chorismate mutase activity, EC 5.4.99.5, and converts chorismate into prephenate. L-Phe binds with positive cooperativity and the binding shifts the protein from dimeric to less active tetrameric and higher oligomeric forms Escherichia coli phenylpyruvate + H2O + CO2
-
 ?

Subunits

Subunits Comment Organism
dimer L-Phe binds with positive cooperativity and the binding shifts the protein from dimeric to less active tetrameric and higher oligomeric forms Escherichia coli
oligomer L-Phe binds with positive cooperativity and the binding shifts the protein from dimeric to less active tetrameric and higher oligomeric forms Escherichia coli
tetramer L-Phe binds with positive cooperativity and the binding shifts the protein from dimeric to less active tetrameric and higher oligomeric forms Escherichia coli

Synonyms

Synonyms Comment Organism
P-protein
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 Escherichia coli