Isolation and Characterization of L-Tryptophan Ammonia Lyase from Rubrivivax benzoatilyticus Strain JA2

Author(s): Ranjith N. Kumavath, Ch.V. Ramana, Ch. Sasikala, Debmalya Barh, Alan Prem Kumar, Vasco Azevedo.

Journal Name: Current Protein & Peptide Science

Volume 16 , Issue 8 , 2015

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Graphical Abstract:


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.

Keywords: Indole-3-acrylic acid, L-tryptophan, L-tryptophan ammonia lyase, Rubrivivax benzoatilyticus JA2.

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Article Details

Year: 2015
Page: [775 - 781]
Pages: 7
DOI: 10.2174/1389203716666150505235929
Price: $58

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