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Literature summary for 4.1.99.1 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

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

Crystallization (Commentary)

Crystallization (Comment) Organism
apo-form of enzyme without bound pyridoxal 5’-phosphate but with two bound sulfate ions, hanging drop vapor diffusion method Escherichia coli
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

Metals/Ions Comment Organism Structure
K+ stabilizing, cold inactivation occurs more slowly in the presence of K+ Escherichia coli
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]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A853
-
-
Escherichia coli JM109 P0A853
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Subunits

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

Temperature Stability [°C]

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

Cofactor

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

pI Value

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