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Literature summary extracted from

  • Lai, J.; Niks, D.; Wang, Y.; Domratcheva, T.; Barends, T.R.; Schwarz, F.; Olsen, R.A.; Elliott, D.W.; Fatmi, M.Q.; Chang, C.E.; Schlichting, I.; Dunn, M.F.; Mueller, L.J.
    X-ray and NMR crystallography in an enzyme active site: the indoline quinonoid intermediate in tryptophan synthase (2011), J. Am. Chem. Soc., 133, 4-7.
    View publication on PubMed

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 Salmonella enterica
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L-tryptophan + glyceraldehyde 3-phosphate + H2O
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?

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.20 Salmonella enterica
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-
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Reaction

EC Number Reaction Comment Organism Reaction ID
4.2.1.20 L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O catalytic mechanism via an indoline quinonoid intermediate, with importance of an equilibrium between tautomeric forms of the substrate, with the protonation state of the major isomer directing the next catalytic step, active site structure, and indoline and beta-site reactions by NMR spectroscopy, overview Salmonella enterica

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
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Salmonella enterica L-tryptophan + glyceraldehyde 3-phosphate + H2O
-
?

Cofactor

EC Number Cofactor Comment Organism Structure
4.2.1.20 pyridoxal 5'-phosphate structure in complex with substrate, overview Salmonella enterica