Synthesis of the Enzymes of the Mandelate Pathway by Pseudomonas putida II. Isolation and Properties of Blocked Mutants

AUTOR(ES)

Hegeman, G. D.

RESUMO

Hegeman, G. D. (University of California, Berkeley). Synthesis of the enzymes of the mandelate pathway by Pseudomonas putida. II. Isolation and properties of blocked mutants. J. Bacteriol. 91:1155–1160. 1966.—Mutants of Pseudomonas putida blocked in early reactions of the pathway for oxidation of d-mandelate were isolated and partially characterized. The specific genetic lesions in these mutants made normal inducer-metabolites of the pathway nonmetabolizable. Under the conditions of gratuitous enzyme synthesis so obtained, it could be shown that the d and l isomers of mandelate are equipotent inducers, and that the synthesis of the first five enzymes of the mandelate pathway is coordinate. Further experiments with the blocked mutants showed that benzoylformate, the third intermediate of the pathway, acts as an inducer without prior conversion to mandelate, and that there is no inducible, concentrating permease for mandelate.

Documentos Relacionados

• Synthesis of the Enzymes of the Mandelate Pathway by Pseudomonas putida III. Isolation and Properties of Constitutive Mutants
• Synthesis of the Enzymes of the Mandelate Pathway by Pseudomonas putida I. Synthesis of Enzymes by the Wild Type
• Isolation and characterization of Pseudomonas aeruginosa mutants blocked in the synthesis of pyoverdin.
• Enzymes of the Tryptophan Synthetic Pathway in Pseudomonas putida
• Antibiotics from Pseudomonas reptilivora II. Isolation, Purification, and Properties1