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Literature summary extracted from

  • Ku, S.Y.; Yip, P.; Howell, P.L.
    Structure of Escherichia coli tryptophanase (2006), Acta Crystallogr. Sect. D, 62, 814-823.
    View publication on PubMed

Application

EC Number Application Comment Organism
4.1.99.1 synthesis production of L-tryptophan and related amino acids Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.99.1 apo-form of enzyme without bound pyridoxal 5’-phosphate but with two bound sulfate ions, hanging drop vapor diffusion method Escherichia coli
4.1.99.1 strong crystal contacts occur on the flat surface of the protein and that the size of crystal contact surface seems to correlate with the diffraction quality of the crystal. The tryptophanase structure, solved in its apo form, does not have covalent PLP bound in the active site, but two sulfate ions. The sulfate ions occupy the phosphoryl-binding site of PLP and the binding site of the alpha-carboxyl of the natural substrate tryptophan. One of the sulfate ions makes extensive interactions with both the transferase and PLP-binding domains of the protein and appears to be responsible for holding the enzyme in its closed conformation Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.99.1 K+ stabilizing, cold inactivation occurs more slowly in the presence of K+ Escherichia coli
4.1.99.1 sulfate two ions bound two the active site of the enzyme, one of the sulfate ions interacts with both the transferase and PLP-binding domains and appears to be responsible for holding the enzyme in its closed conformation Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.99.1 52000
-
 4 * 52000 Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.99.1 L-Trp + H2O Escherichia coli
-
 indole + pyruvate + NH4+
-
 r
4.1.99.1 L-Trp + H2O Escherichia coli JM109
-
 indole + pyruvate + NH4+
-
 r

Organism

EC Number Organism UniProt Comment Textmining
4.1.99.1 Escherichia coli P0A853
-
-
4.1.99.1 Escherichia coli JM109 P0A853
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.99.1 no added pyridoxal 5’-phosphate during purification procedure resulting in the inactive apo-form of the enzyme Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.99.1 D-Trp + H2O in the presence of high concentrations of ammonium phosphate Escherichia coli indole + pyruvate + NH4+
-
 ?
4.1.99.1 D-Trp + H2O in the presence of high concentrations of ammonium phosphate Escherichia coli JM109 indole + pyruvate + NH4+
-
 ?
4.1.99.1 L-Trp + H2O
-
 Escherichia coli indole + pyruvate + NH4+
-
 r
4.1.99.1 L-Trp + H2O
-
 Escherichia coli JM109 indole + pyruvate + NH4+
-
 r

Subunits

EC Number Subunits Comment Organism
4.1.99.1 dimer inactive, formed upon cold incubation or purification Escherichia coli
4.1.99.1 tetramer 4 * 52000 Escherichia coli

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4.1.99.1 additional information
-
 inactivation of the enzyme at low temperatures due to dissociation of the active tetramer into dimers upon cold incubation Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.99.1 pyridoxal 5'-phosphate dependent on Escherichia coli
4.1.99.1 pyridoxal 5'-phosphate covalent binding required to activate the enzyme Escherichia coli

pI Value

EC Number Organism Comment pI Value Maximum pI Value
4.1.99.1 Escherichia coli calculated from the deduced amino acid sequence
-
 6.2