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- Name help_outline L-tryptophan Identifier CHEBI:57912 Charge 0 Formula C11H12N2O2 InChIKeyhelp_outline QIVBCDIJIAJPQS-VIFPVBQESA-N SMILEShelp_outline [NH3+][C@@H](Cc1c[nH]c2ccccc12)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 57 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (E)-3-(indol-3-yl)acrylate Identifier CHEBI:131929 Charge -1 Formula C11H8NO2 InChIKeyhelp_outline PLVPPLCLBIEYEA-AATRIKPKSA-M SMILEShelp_outline C1(=CNC2=C1C=CC=C2)\C=C\C(=O)[O-] 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline NH4+ Identifier CHEBI:28938 (CAS: 14798-03-9) help_outline Charge 1 Formula H4N InChIKeyhelp_outline QGZKDVFQNNGYKY-UHFFFAOYSA-O SMILEShelp_outline [H][N+]([H])([H])[H] 2D coordinates Mol file for the small molecule Search links Involved in 529 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:41259 | RHEA:41260 | RHEA:41261 | RHEA:41262 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Isolation and Characterization of L-Tryptophan Ammonia Lyase from Rubrivivax benzoatilyticus Strain JA2.
Kumavath R.N., Ramana C.h.V., Sasikala C.h., Barh D., Kumar A.P., Azevedo V.
Ammonia lyase belongs to the family of enzymes that catalyzes the deamination of amino acids. Depending on the relative activity towards the substrates, L-tryptophan ammonia lyase converts L-tryptophan to indole 3-acrylic acid and ammonia. Here, we isolated, purified, and characterized an L-trypto ... >> More
Ammonia lyase belongs to the family of enzymes that catalyzes the deamination of amino acids. Depending on the relative activity towards the substrates, L-tryptophan ammonia lyase converts L-tryptophan to indole 3-acrylic acid and ammonia. Here, we isolated, purified, and characterized an L-tryptophan ammonia lyase from phototrophic purple non-sulfur bacterium Rubrivivax benzoatilyticus JA2. The isolated L-tryptophan ammonia lyase found to catalyze the reaction of L-tryptophan to produce indole 3-acrylic acid and NH3. The enzyme is a heterotetramer and has the highest affinity to L-tryptophan. The optimum pH and temperature for the enzymatic action were 7.5 and 35°C, respectively and the Km and Vmax were 40.4 ± 23.1 nM and 0.964±0.2046 s(-1), respectively. These results suggest that the isolated enzyme is highly bioactive and could be a new class. Further molecular analyses are required to confirm the novelty of the enzyme. << Less