The enzyme, characterized from the bacterium Rubrivivax benzoatilyticus JA2, requires no cofactors. It acts on L-phenylalanine and L-glutamate with about 60% of the activity with L-tryptophan, and on L-tyrosine, glycine, and L-alanine with about 30% of the activity.
Kumavath, R.N., Ramana ChV., Sasikala Ch, Barh, D., Kumar, A.P. and Azevedo, V. Isolation and characterization of L-tryptophan ammonia lyase from Rubrivivax benzoatilyticus strain JA2. Curr Protein Pept Sci16 (2015) 775–781. [PMID: 25961404]