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Literature summary for 4.2.1.20 extracted from

  • Jeong, M.S.; Jeong, J.K.; Park, K.S.; Kim, H.T.; Lee, K.M.; Lim, W.K.; Jang, S.B.
    Crystallization and preliminary X-ray analysis of tryptophan synthase alpha-subunits from Escherichia coli (2004), Acta Crystallogr. Sect. D, 60, 132-134.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of the alpha-subunit in strain RB797 Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
10 mg/ml purified recombinant alpha-subunit, hanging drop vapour diffusion method, 298K, equal volume, 0.001 ml, of protein solution and reservoir solution are mixed and placed over 0.5 ml reservoir solution, precipitant solution: 0.5 M ammonium sulfate, 0.1 M trisodium citrate dihydrate, 1.0 M lithium sulfate monohydrate, pH 5.6, first crystals after 7-10 days, maximal size within 2 weeks, X-ray diffraction structure determination and analysis at 2.8 A resolution Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant alpha-subunit Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O also catalyses the conversion of serine and indole into tryptophan and water, and of indoleglycerol phosphate into indole and glyceraldehyde phosphate (the latter reaction was listed formerly as EC 4.2.1.8) Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-(indol-3-yl)glycerol 3-phosphate alpha-subunit of the bienzyme complex, alpha-reaction Escherichia coli D-glyceraldehyde 3-phosphate + indole channeling of indole to the beta-subunit active site ?
L-serine + indole beta-subunit of the bienzyme complex, beta-reaction Escherichia coli L-tryptophan + H2O
-
?

Subunits

Subunits Comment Organism
More the alpha-subunit contains no disulfide bond, conformational stabilization mechanism Escherichia coli
tetramer alpha2beta2 enzyme complex Escherichia coli

Synonyms

Synonyms Comment Organism
alphaTS alpha-subunit Escherichia coli

Cofactor

Cofactor Comment Organism Structure
additional information the alpha-subunit contains no prosthetic group Escherichia coli