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Literature summary extracted from

  • Dunn, M.F.
    Allosteric regulation of substrate channeling and catalysis in the tryptophan synthase bienzyme complex (2012), Arch. Biochem. Biophys., 519, 154-166.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.20 L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate Escherichia coli the tryptophan synthase alpha2beta2 bi-enzyme complex catalyzes the last two steps in the synthesis of L-tryptophan (L-Trp). The alpha-subunit catalyzes cleavage of 3-indole-D-glycerol 3'-phosphate to give indole and D-glyceraldehyde 3'-phosphate. Indole is then transferred from the alpha-subunit to the beta-subunit where it reacts with L-Ser in a pyridoxal 5'-phosphate-dependent reaction to give L-Trp and a water molecule L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
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Organism

EC Number Organism UniProt Comment Textmining
4.2.1.20 Escherichia coli
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-
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.20 L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate the tryptophan synthase alpha2beta2 bi-enzyme complex catalyzes the last two steps in the synthesis of L-tryptophan (L-Trp). The alpha-subunit catalyzes cleavage of 3-indole-D-glycerol 3'-phosphate to give indole and D-glyceraldehyde 3'-phosphate. Indole is then transferred from the alpha-subunit to the beta-subunit where it reacts with L-Ser in a pyridoxal 5'-phosphate-dependent reaction to give L-Trp and a water molecule Escherichia coli L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
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Subunits

EC Number Subunits Comment Organism
4.2.1.20 heterotetramer
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Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
4.2.1.20 pyridoxal 5'-phosphate dependent on Escherichia coli