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Literature summary for 4.1.99.1 extracted from

  • Rety, S.; Deschamps, P.; Leulliot, N.
    Structure of Escherichia coli tryptophanase purified from an alkaline-stressed bacterial culture (2015), Acta Crystallogr. Sect. F, 71, 1378-1383 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.1.99.1

Cloned(Commentary)

Cloned (Comment) Organism
gene tnaA, recombinant overexpression of the enzyme in Escherichia coli strain Rosetta (DE3) pLysS Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant apo-enzyme in an open conformation, hanging drop vapour diffusion method with 25-30% PEG 4000, 30 mM ammonium sulfate, 20 mM 2-mercaptoethanol, 100 mM Tris-HCl, pH 9.0, X-ray diffraction structur determination and analysis at 2.8 A resolution Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
K+ required Escherichia coli
additional information monovalent cations (K+ or NH4 + ) are required for the binding of PLP to a lysine residue in the active site, leading to the functionally active form Escherichia coli
NH4+ required Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-tryptophan + H2O Escherichia coli Tnase can act in reverse to form L-tryptophan at high concentrations of pyruvate and ammonia indole + pyruvate + NH3
-
 r

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A853
-
-

Purification (Commentary)

Purification (Comment) Organism
gene tnaA, recombinant enzyme from Escherichia coli strain Rosetta (DE3) pLysS by ammnoium sulfate fractionation, dialysis, anion exchange and hydrophobic interaction chromatography, followed by preparative gel filtration, and ultrafiltration Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
L-tryptophan + H2O = indole + pyruvate + NH3 catalyses the reaction in which L-tryptophan is degraded to indole, pyruvate and ammonia via alpha,beta-elimination and beta-replacement mechanisms Escherichia coli
a

Source Tissue

Source Tissue Comment Organism Textmining
additional information tryptophanase is often overexpressed in stressed cultures Escherichia coli
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-tryptophan + H2O Tnase can act in reverse to form L-tryptophan at high concentrations of pyruvate and ammonia Escherichia coli indole + pyruvate + NH3
-
 r

Subunits

Subunits Comment Organism
homotetramer 4 * 52800, SDS-PAGE Escherichia coli
More peptide mass-fingerprinting of purified recombinant enzyme, mass spectrometry Escherichia coli

Synonyms

Synonyms Comment Organism
TNase
-
 Escherichia coli
tryptophan indole-lyase
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
 assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
 assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate dependent on, monovalent cations (K+ or NH4+) are required for the binding of pyridoxal 5'-phosphate to a lysine residue in the active site, leading to the functionally active form. Each monomer binds one molecule of pyridoxal 5'-phosphate, which forms an aldimine bond to the Lys270 residue in the active site Escherichia coli

Expression

Organism Comment Expression
Escherichia coli tryptophanase is often overexpressed in stressed cultures, e.g. under alkaline stress up

General Information

General Information Comment Organism
physiological function tryptophanase is a bacterial enzyme involved in the degradation of tryptophan to indole, pyruvate and ammonia, which are compounds that are essential for bacterial survival. Tryptophanase is often overexpressed in stressed cultures Escherichia coli