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Literature summary extracted from

  • Miles, E.W.
    Tryptophan synthase, structure, function, and protein engineering (1995), Subcell. Biochem., 24, 207-254.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.2.1.20 structure and function of alpha subunit, beta subunit, alpha2beta2 complex Salmonella enterica subsp. enterica serovar Typhimurium

Protein Variants

EC Number Protein Variants Comment Organism
4.2.1.20 D60Y mutation inhibits the ligand-induced transition of the alpha subunit from an open to a closed conformation that serves to block the tunnel for the metabolite chanelling Salmonella enterica subsp. enterica serovar Typhimurium
4.2.1.20 E109A catalytic activity with beta-chloro-L-Ala, but negligible activity with L-Ser, beta subunit Salmonella enterica subsp. enterica serovar Typhimurium
4.2.1.20 E109D catalytic activity with beta-chloro-L-Ala, but reduced activity with L-Ser, beta subunit Salmonella enterica subsp. enterica serovar Typhimurium
4.2.1.20 E49F mutation inhibits the ligand-induced transition of the alpha subunit from an open to a closed conformation that serves to block the tunnel for the metabolite chanelling Salmonella enterica subsp. enterica serovar Typhimurium
4.2.1.20 G281R reduced activity and weak association with alpha subunit Escherichia coli
4.2.1.20 G51L mutation inhibits the ligand-induced transition of the alpha subunit from an open to a closed conformation that serves to block the tunnel for the metabolite chanelling Salmonella enterica subsp. enterica serovar Typhimurium
4.2.1.20 K87T Lys87 represents an essential catalytic residue as acceptor of the alpha-proton of L-Ser, alpha subunit Salmonella enterica subsp. enterica serovar Typhimurium
4.2.1.20 P132A increase of activity of the alpha2beta2 complex Escherichia coli
4.2.1.20 P132G increase of activity of the alpha2beta2 complex Escherichia coli
4.2.1.20 P57A increase of activity of the alpha2beta2 complex Escherichia coli
4.2.1.20 R179L mutation inhibits the ligand-induced transition of the alpha subunit from an open to a closed conformation that serves to block the tunnel for the metabolite chanelling Salmonella enterica subsp. enterica serovar Typhimurium

General Stability

EC Number General Stability Organism
4.2.1.20 pyridoxal 5'-phosphate strongly stabilizes beta2 subunit Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.20 Escherichia coli
-
-
-
4.2.1.20 Salmonella enterica subsp. enterica serovar Typhimurium
-
-
-

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 mechanism Salmonella enterica subsp. enterica serovar Typhimurium
a
4.2.1.20 L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O mechanism Escherichia coli
a

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 + L-serine
-
 Salmonella enterica subsp. enterica serovar Typhimurium L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
-
 ?
4.2.1.20 1-(indol-3-yl)glycerol 3-phosphate + L-serine
-
 Escherichia coli L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
-
 ?
4.2.1.20 indole + D-glyceraldehyde 3-phosphate r Salmonella enterica subsp. enterica serovar Typhimurium indole-3-glycerol phosphate r ?
4.2.1.20 indole + D-glyceraldehyde 3-phosphate r Escherichia coli indole-3-glycerol phosphate r ?
4.2.1.20 indole + L-serine
-
 Salmonella enterica subsp. enterica serovar Typhimurium L-tryptophan + H2O
-
 ?
4.2.1.20 indole + L-serine
-
 Escherichia coli L-tryptophan + H2O
-
 ?
4.2.1.20 indole-3-glycerol phosphate r Salmonella enterica subsp. enterica serovar Typhimurium indole + D-glyceraldehyde 3-phosphate r ?
4.2.1.20 indole-3-glycerol phosphate r Escherichia coli indole + D-glyceraldehyde 3-phosphate r ?
4.2.1.20 indole-3-glycerol phosphate mechanism Salmonella enterica subsp. enterica serovar Typhimurium indole + D-glyceraldehyde 3-phosphate r ?

Subunits

EC Number Subunits Comment Organism
4.2.1.20 More activities of alpha and beta subunits are coordinated by allosteric interactions Salmonella enterica subsp. enterica serovar Typhimurium
4.2.1.20 More activities of alpha and beta subunits are coordinated by allosteric interactions Escherichia coli

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4.2.1.20 additional information
-
 pyridoxal 5'-phosphate stabilizes against thermal inactivation, Schiff-base forming amino acids destabilize holo beta subunit Escherichia coli
4.2.1.20 additional information
-
 ligands that promote subunit association (L-Ser, L-Trp, D-Trp) raise the inactivation temperature of alpha subunit Salmonella enterica subsp. enterica serovar Typhimurium
4.2.1.20 additional information
-
 denaturation temperatures of alpha subunit Salmonella enterica subsp. enterica serovar Typhimurium
4.2.1.20 additional information
-
 denaturation temperatures of alpha subunit Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
4.2.1.20 pyridoxal 5'-phosphate
-
 Escherichia coli
4.2.1.20 pyridoxal 5'-phosphate forms a Schiff base with the epsilon amino-group of Lys87 Salmonella enterica subsp. enterica serovar Typhimurium