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
-
4.1.99.1
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quinonoid
-
transposase
-
aldimine
-
proteus
-
phenol-lyase
-
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
-
phillips
-
alvei
-
analysis
-
food industry
-
biotechnology
-
drug development
-
medicine
-
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
4.1.99.1 tryptophanaseAdvanced search results
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results (Metals Ions
Metals Ions on EC 4.1.99.1 - tryptophanase
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METALS and IONS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Cl-
-
bound to enzyme, possibly required for stabilization of subunit interactions
K+
NH4+
Rb+
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
Tl+
additional information
K+
-
kinetics of tryptophanase inactivation/activation by sudden removal/addition of K+ with the aid of a crown ether or cryptand
K+
-
promotes the conversion of the inactive holoenzyme into the active holoenzyme rather than being involved in the conversion of the apoenzyme and pyridoxal 5'-phosphate into the active holoenzyme
K+
monovalent cation required for activity and for tight cofactor binding
K+
stabilizing, cold inactivation occurs more slowly in the presence of K+
NH4+
-
promotes the conversion of the inactive holoenzyme into the active holoenzyme rather than being involved in the conversion of the apoenzyme and pyridoxal 5'-phosphate into the active holoenzyme
NH4+
monovalent cation required for activity and for tight cofactor binding
Tl+
monovalent cation required for activity and for tight cofactor binding
additional information
monovalent cations (K+ or NH4 + ) are required for the binding of PLP to a lysine residue in the active site, leading to the functionally active form
additional information
-
monovalent cations (K+ or NH4 + ) are required for the binding of PLP to a lysine residue in the active site, leading to the functionally active form
additional information
the enzyme requires a monovalent cation, either K+, NH4+, Rb+ or Cs+ for activity, with Na+ and Li+ giving little or no activity
additional information
the enzyme requires a monovalent cation, either K+, NH4+, Rb+ or Cs+ for activity, with Na+ and Li+ giving little or no activity
