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Literature summary for 4.2.1.20 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
Search for more literature for 4.2.1.20

Cloned(Commentary)

Cloned (Comment) Organism
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

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

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant alpha-subunits of wild-type and mutant enzymes 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
a

Renatured (Commentary)

Renatured (Comment) Organism
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]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
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)

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
-
 ?
L-serine + indole beta-subunit of the bienzyme complex, beta-reaction Escherichia coli L-tryptophan + H2O
-
 ?

Subunits

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

Synonyms

Synonyms Comment Organism
alphaTS
-
 Escherichia coli