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Literature summary for 4.1.99.1 extracted from

  • Tsesin, N.; Kogan, A.; Gdalevsky, G.Y.; Himanen, J.P.; Cohen-Luria, R.; Parola, A.H.; Goldgur, Y.; Almog, O.
    The structure of apo tryptophanase from Escherichia coli reveals a wide-open conformation (2007), Acta Crystallogr. Sect. D, D63, 969-974.
    View publication on PubMed
Search for more literature for 4.1.99.1

Application

Application Comment Organism
drug development enzyme might serve as a target for antibiotics Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
apo-form of the enzyme, hanging drop vapor diffusion method Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Cl- bound to enzyme, possibly required for stabilization of subunit interactions Escherichia coli
K+ monovalent cation required for activity Escherichia coli
Mg2+ bound to enzyme Escherichia coli
NH4+ monovalent cation required for activity Escherichia coli
Tl+ monovalent cation required for activity Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
52800
-
 4 * 52800 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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
tetramer 4 * 52800 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate one molecule bound per monomer Escherichia coli