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Literature summary extracted from

  • Kim, J.W.; Kim, E.Y.; Park, H.H.; Jung, J.E.; Kim, H.D.; Shin, H.J.; Lim, W.K.
    Homodimers of mutant tryptophan synthase alpha-subunits in Escherichia coli (2001), Biochem. Biophys. Res. Commun., 289, 568-572.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.20 expression of wild-type and mutant F139W, T24M/F139W, and T24L/F139W alpha-subunits as monomers, expression of mutant T24A/F139W, T24S/F139W and T24K/F139W alpha-subunits as soluble dimers in strain RB797 Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
4.2.1.20 F139W oligonucleotide-directed mutagenesis, recombinant alpha-subunit mutant, forms monomers Escherichia coli
4.2.1.20 T24A/F139W oligonucleotide-directed mutagenesis, recombinant alpha-subunit mutant, forms dimers Escherichia coli
4.2.1.20 T24K/F139W oligonucleotide-directed mutagenesis, recombinant alpha-subunit mutant, forms dimers Escherichia coli
4.2.1.20 T24L/F139W oligonucleotide-directed mutagenesis, recombinant alpha-subunit mutant, forms monomers Escherichia coli
4.2.1.20 T24M/F139W oligonucleotide-directed mutagenesis, recombinant alpha-subunit mutant, forms monomers Escherichia coli
4.2.1.20 T24S/F139W oligonucleotide-directed mutagenesis, recombinant alpha-subunit mutant, forms dimers Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.2.1.20 additional information
-
 additional information dissociation constants of the beta-subunit combined with the different subunits of wild-type and mutants Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.20 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.1.20 recombinant alpha-subunits of wild-type and mutant enzymes Escherichia coli

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 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
a

Renatured (Commentary)

EC Number Renatured (Comment) Organism
4.2.1.20 denaturation of recombinant wild-type and mutant alpha-subunit monomers and dimers with urea, refolding of all forms as monomers Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.2.1.20 additional information
-
 activity of the beta-subunit combined with the different alpha-subunit monomers and dimers of wild-type and mutants Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.20 1-(indol-3-yl)glycerol 3-phosphate alpha-subunit of the bienzyme complex, alpha-reaction Escherichia coli D-glyceraldehyde 3-phosphate + indole
-
 ?
4.2.1.20 L-serine + indole beta-subunit of the bienzyme complex, beta-reaction Escherichia coli L-tryptophan + H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
4.2.1.20 More dimer formation seems to be associated with the formation of protein aggregates in vivo Escherichia coli
4.2.1.20 tetramer alpha2beta2 enzyme complex Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
4.2.1.20 alphaTS
-
 Escherichia coli