Abstract
A method for the preparation of a 50 fold purified enzyme from Vicia faba catalyzing the non-oxidative deamination of histidine to imidazole propionic acid and ammonia is described. AMP and B 12 requirement for the purified enzyme is indicated. The enzyme exhibited optimal activity at pH 9.0 in pyrophosphate buffer. Km values for L-histidine, AMP and B 12 were found to be 4.0 mM, 6.2 mM and 0.97 mM, respectively. Chromatographic analysis and the stoichiometric relationship between enzymatically liberated ammonia and product formed suggested that the enzymatic product is imidazole propionic acid.
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