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4.1.99.1: tryptophanase

This is an abbreviated version!
For detailed information about tryptophanase, go to the full flat file.

Word Map on EC 4.1.99.1

Reaction

L-tryptophan
+
H2O
=
indole
 +
pyruvate
 +
NH3

Synonyms

L-tryptophan indole-lyase, L-tryptophanase, TIL, tna2, TnaA, tnaA2, TNase, Tpase, Trpase, tryptophan indole lyase, tryptophan indole-lyase, tryptophan-indole lyase, tryptophanase, tryptophanase 2, VcTrpase

ECTree

     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.99 Other carbon-carbon lyases
                4.1.99.1 tryptophanase

General Stability

General Stability on EC 4.1.99.1 - tryptophanase

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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
activity decreases at pressures above 50 MPa, and by 100 MPa is less than 10% of the activity at 1 bar, initial increase in activity with pressure, reaching a maximum of about 140% at 30 MPa.
-
greater than 90% activity remaining at 100 MPa, initial increase in activity with pressure, reaching a maximum of about 140% at 60 MPa.
immobilized enzyme shows higher thermal stability and resistance to a denaturing agent such as guanidine-HCl than the soluble enzyme
-
rapid inactivation by visible light irradiation in presence of pyridoxal 5'-phosphate. Photoinactivation follows pseudo-first-order kinetics
-
repeated slow freezing at -20°C and subsequent thawing at room temperature causes the enzyme to aggregate
-
when used repeatedly in a batch system or continously in a flow system in the absence of added pyridoxal 5'-phosphate, immobilized holo-tryptophanase gradually loses its original activity, pyridoxal 5'-phosphate restores its initial activity
-