Enzymes of the Tryptophan Synthetic Pathway in Pseudomonas putida

摘要: The first four enzymatic activities of the tryptophan synthetic pathway in Pseudomonas putida were found on separate molecules. Gel filtration and density gradient centrifugation experiments did not disclose any associations or aggregations among them. These findings contrast with situation enteric bacteria, where two are an aggregate third fourth catalyzed by a single enzyme. Tryptophan synthetase, last enzyme pathway, consists dissociable components. affinity these components is less P. than case Escherichia coli.