Enzymes of the tryptophan synthetic pathway in Pseudomonas putida.
J Bacteriol
; 95(1): 107-12, 1968 Jan.
Article
em En
| MEDLINE
| ID: mdl-5636809
ABSTRACT
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 the situation found in the enteric bacteria, where the first two activities are found in an aggregate and the third and fourth are catalyzed by a single enzyme. Tryptophan synthetase, the last enzyme of the pathway, consists of two dissociable components. The affinity of these components is less in P. putida than is the case in Escherichia coli.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Pseudomonas
/
Triptofano
Idioma:
En
Revista:
J Bacteriol
Ano de publicação:
1968
Tipo de documento:
Article