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
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4.1.99.1
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quinonoid
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transposase
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aldimine
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proteus
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phenol-lyase
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thermonuclease
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beta-elimination
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l-trp
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tryptophan-induced
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antitermination
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pyridoxal-p
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rho-dependent
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rapid-scanning
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phillips
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alvei
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analysis
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food industry
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biotechnology
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drug development
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medicine
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synthesis
- 4.1.99.1
-
quinonoid
- transposase
-
aldimine
- proteus
-
phenol-lyase
- thermonuclease
-
beta-elimination
- l-trp
-
tryptophan-induced
-
antitermination
-
pyridoxal-p
-
rho-dependent
-
rapid-scanning
-
phillips
- alvei
- analysis
- food industry
- biotechnology
- drug development
- medicine
- synthesis
Reaction
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
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General Stability
General Stability on EC 4.1.99.1 - tryptophanase
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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.
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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
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rapid inactivation by visible light irradiation in presence of pyridoxal 5'-phosphate. Photoinactivation follows pseudo-first-order kinetics
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repeated slow freezing at -20°C and subsequent thawing at room temperature causes the enzyme to aggregate
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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
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