Characterization of carbamoyl phosphate synthetase of Streptomyces spp.
Indian J Exp Biol
;
2000 Sep; 38(9): 931-5
Article
in English
| 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).
Full text:
Available
Index:
IMSEAR (South-East Asia)
Main subject:
Arginine
/
Radiometry
/
Streptomyces
/
Uracil
/
Carbamyl Phosphate
/
Gene Expression Regulation, Bacterial
/
Colorimetry
/
Carbon-Nitrogen Ligases with Glutamine as Amide-N-Donor
/
Allosteric Regulation
/
Escherichia coli
Language:
English
Journal:
Indian J Exp Biol
Year:
2000
Type:
Article
Similar
MEDLINE
...
LILACS
LIS