Literature summary for 4.1.99.1 extracted from

Kogan, A.; Raznov, L.; Gdalevsky, G.; Cohen-Luria, R.; Almog, O.; Parola, A.; Goldgur, Y.
Structures of Escherichia coli tryptophanase in holo and semi-holo forms (2015), Acta Crystallogr. Sect. F, 71, 286-290 .

Cloned(Commentary)

Cloned (Comment)	Organism
recombinant enzyme overexpression in Escherichia coli strain SVS 370	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant tryptophanase in holo- and semi-holoforms, hanging drop vapour diffusion method, mixing of 15-25 mg/ml protein in 50 mM sodium phosphate, pH 6.0, 5 mM 2-mercaptoethanol, and 0.5-2 mM pyridoxal 5'-phosphate in a ratio of 3:1 with precipitant solution containing 10-15% w/v ammonium sulfate, 25 mM potassium acetate, pH 5.4, and 3-10 mM2-mercaptoethanol, 2-7 days, X-ray diffraction structure determination and analysis at 2.9-3.2 A resolution, both crystal forms belong to the same space group P43212 but have slightly different unit-cell parameters, molecular replacement using the structure of apo Trpase, PDB ID 2oqx, as the search model	Escherichia coli

Crystallization (Comment)

Organism

purified recombinant tryptophanase in holo- and semi-holoforms, hanging drop vapour diffusion method, mixing of 15-25 mg/ml protein in 50 mM sodium phosphate, pH 6.0, 5 mM 2-mercaptoethanol, and 0.5-2 mM pyridoxal 5'-phosphate in a ratio of 3:1 with precipitant solution containing 10-15% w/v ammonium sulfate, 25 mM potassium acetate, pH 5.4, and 3-10 mM2-mercaptoethanol, 2-7 days, X-ray diffraction structure determination and analysis at 2.9-3.2 A resolution, both crystal forms belong to the same space group P43212 but have slightly different unit-cell parameters, molecular replacement using the structure of apo Trpase, PDB ID 2oqx, as the search model

Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
L-tryptophan + H2O	Escherichia coli	-	indole + pyruvate + NH3	-	r

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0A853	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-tryptophan + H2O	-	Escherichia coli	indole + pyruvate + NH3	-	r

Subunits

Subunits	Comment	Organism
More	of the two subunits in the asymmetric unit, one is found in the holoform, while the other appears to be in the apoform in a wide-open conformation with two sulfate ions bound in the vicinity of the active site. Enzyme Trpase is flexible in the apoform	Escherichia coli

Synonyms

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

Cofactor

Cofactor	Comment	Organism	Structure
pyridoxal 5'-phosphate	dependent on	Escherichia coli

General Information

General Information	Comment	Organism
evolution	enzyme Trpase is classified as beta-eliminating lyase	Escherichia coli
additional information	the conformation of all holo subunits is the same in both crystal forms. The structures suggest that Trpase is flexible in the apoform. Its conformation partially closes upon binding of PLP. The closed conformation might correspond to the enzyme in its active state with both cofactor and substrate bound in a similar way as in tyrosine phenol-lyase	Escherichia coli