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
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quinonoid
- transposase
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aldimine
- proteus
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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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Cofactor
Cofactor on EC 4.1.99.1 - tryptophanase
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pyridoxal 5'-phosphate
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contains 4 mol of pyridoxal 5'-phosphate per mol of enzyme
pyridoxal 5'-phosphate
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contains 4 mol of pyridoxal 5'-phosphate per mol of enzyme
pyridoxal 5'-phosphate
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some coenzyme analogues can replace pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
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enzyme contains 4 mol of pyridoxal 5'-phosphate per mol of enzyme at pH 6.8 and 3 mol of pyridoxal 5'-phosphate per mol of enzyme at pH 7.8 in K+ buffer
pyridoxal 5'-phosphate
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enzyme contains 4 mol of pyridoxal 5'-phosphate per mol of enzyme at pH 6.8 and 3 mol of pyridoxal 5'-phosphate per mol of enzyme at pH 7.8 in K+ buffer
pyridoxal 5'-phosphate
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enzyme contain 4 mol of pyridoxal 5'-phosphate per mol of enzyme, independently of the pH in presence of K+
pyridoxal 5'-phosphate
Escherichia aurescens
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enzyme contain 4 mol of pyridoxal 5'-phosphate per mol of enzyme, independently of the pH in presence of K+
pyridoxal 5'-phosphate
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conversion of apoenzyme into the active holoenzyme is attained at 30°C in Tris-HCl buffer, pH 8.0, containing pyridoxal 5'-phosphate and K+, no conversion occurs at 5°C
pyridoxal 5'-phosphate
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one enzyme molecule contains 4 pyridoxal 5'-phosphate combining sites
pyridoxal 5'-phosphate
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one enzyme molecule contains 4 pyridoxal 5'-phosphate combining sites
pyridoxal 5'-phosphate
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one enzyme molecule contains 4 pyridoxal 5'-phosphate combining sites
pyridoxal 5'-phosphate
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one enzyme molecule contains 4 pyridoxal 5'-phosphate combining sites
pyridoxal 5'-phosphate
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enzyme contains 2 pyridoxal 5'-phosphate per subunit
pyridoxal 5'-phosphate
covalent binding required to activate the enzyme
pyridoxal 5'-phosphate
dependent on, monovalent cations (K+ or NH4+) are required for the binding of pyridoxal 5'-phosphate to a lysine residue in the active site, leading to the functionally active form. Each monomer binds one molecule of pyridoxal 5'-phosphate, which forms an aldimine bond to the Lys270 residue in the active site
pyridoxal 5'-phosphate
dependent on, residue Arg103 plays an important role in orientation of the cofactor pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
dependent on, the active site residues involved in cofactor binding are highly conserved for enzyme TIL
pyridoxal 5'-phosphate
dependent on, the active site residues involved in cofactor binding are highly conserved for enzyme TIL
pyridoxal 5'-phosphate
dependent on, the activity of TPase can be modulated by the concentration of pyridoxal 5'-phosphate