Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.95 L-serine feedback regulation, positive and negative cooperativity in absence of NADH, positive in presence of NADH, overview Escherichia coli
1.1.1.95 additional information the enzyme contains an ACT domain, which is involved in the allosteric regulation mechanism Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.95 3-phospho-D-glycerate + NAD+ Escherichia coli first step in biosynthesis of L-serine, the enzyme contains an ACT domain, which is involved in the allosteric regulation mechanism, residue W139 is involved 3-phosphohydroxypyruvate + NADH
-
 ?
4.2.1.51 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
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.95 Escherichia coli P0A9T0
-
-
4.2.1.51 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.95 3-phospho-D-glycerate + NAD+ first step in biosynthesis of L-serine, the enzyme contains an ACT domain, which is involved in the allosteric regulation mechanism, residue W139 is involved Escherichia coli 3-phosphohydroxypyruvate + NADH
-
 ?
1.1.1.95 3-phospho-D-glycerate + NAD+ D-isomer-specific Escherichia coli 3-phosphohydroxypyruvate + NADH
-
 ?
4.2.1.51 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
-
 ?
4.2.1.51 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

EC Number Subunits Comment Organism
1.1.1.95 More the enzyme contains an ACT domain, which is involved in the allosteric regulation mechanism Escherichia coli
4.2.1.51 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
4.2.1.51 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
4.2.1.51 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

EC Number Synonyms Comment Organism
1.1.1.95 3PGDH
-
 Escherichia coli
1.1.1.95 More the enzyme belongs to the D-isomer-specific 2-hydroxyacid dehydrogenase family Escherichia coli
4.2.1.51 P-protein
-
 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.95 NAD+ cofactor binding structure Escherichia coli