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Literature summary for 4.1.99.1 extracted from

  • Almog, O.; Kogan, A.; de Leeuw, M.; Gdalevsky, G.Y.; Cohen-Luria, R.; Parola, A.H.
    Structural insights into cold inactivation of tryptophanase and cold adaptation degrees of subtilisin S41: Minireview (2008), Biopolymers, 89, 354-359.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
K+ monovalent cation required for activity and for tight cofactor binding Escherichia coli
NH4+ monovalent cation required for activity and for tight cofactor binding Escherichia coli
Tl+ monovalent cation required for activity and for tight cofactor binding 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

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A853
-
-

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
dimer inactive dimer formed upon cold incubation, process reversible Escherichia coli
tetramer 4 * 52000 Escherichia coli

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2
-
reversible inactivation followed by a dissociation into dimers Escherichia coli

Cofactor

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