Characterization of carbamoyl phosphate synthetase of Streptomyces spp.
Indian J Exp Biol
;
2000 Sep; 38(9): 931-5
Artículo
en Inglés
| IMSEAR
| ID: sea-61184
ABSTRACT
Carbamoyl phosphate synthetase (CPS) activity in Streptomyces lividans was repressed (70%) by addition of arginine and uracil in the growth medium. Enzyme activity was also inhibited by UMP and activated by ornithine and IMP. Pattern of inhibition and activation was similar irrespective of whether the cells were grown in medium supplemented with arginine or with uracil. A mutant of S. coelicolor with dual auxotrophy for arginine and uracil possessed only about 20% of CPS activity compared to the wild-type strain. An activity staining protocol has been developed for CPS enzyme. Using this method a single CPS band has been observed in the crude extracts of Escherichia coli as well as in S. lividans. Taken together, our results supported the conclusion that Streptomyces species might possess a single CPS enzyme unlike other gram-positive bacteria, which show the presence of two pathway-specific isozymes (Bacillus) or none (Lactobacillus and Leuconostoc).
Texto completo:
Disponible
Índice:
IMSEAR (Asia Sudoriental)
Asunto principal:
Arginina
/
Radiometría
/
Streptomyces
/
Uracilo
/
Carbamoil Fosfato
/
Regulación Bacteriana de la Expresión Génica
/
Colorimetría
/
Ligasas de Carbono-Nitrógeno con Glutamina como Donante de Amida-N
/
Regulación Alostérica
/
Escherichia coli
Idioma:
Inglés
Revista:
Indian J Exp Biol
Año:
2000
Tipo del documento:
Artículo
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