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Inhibition of nitrite reductase and urease by arginine and proline in the cyanobacterium Anabaena cycadeae

โœ Scribed by Surendra Singh; Prof. P. S. Bisen


Publisher
John Wiley and Sons
Year
1994
Tongue
English
Weight
298 KB
Volume
34
Category
Article
ISSN
0233-111X

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โœฆ Synopsis


The arginine and proline inhibition of nitrite reductase and urease activities have been studied in the cyanobacterium Anabaena cycadeae and its mutant strain lacking glutamine synthetase (GS)') activity. Arginine and proline inhibited the nitrite reductase and urease activities in the parent strain, however, they could not do so in the mutant strain. The level of arginine-and proline-dependent NH: production in the outer medium was several fold higher in the mutant strain as compared to its parent strain. These results suggest that (1) nitrite reductase and urease activities are arginine-and proline-repressible;

(2) the catalytic function of GS is necessarily required for the arginine and proline inhibition of nitrite reductase and urease systems; and (3) the NH: resulting from the catabolism of arginine and proline should be metabolized via GS for repression of nitrite reductase and urease to occur. I ) Abbreviations: GOGAT, glutamate synthase; GS, glutamine synthetase; Hepes, 4-(2-hydroxyethyl)-1 -piperazineethane sulphonic acid; MTA, mixed alkyltrimethyl ammonium bromide; MOPS, 3-(N-morpholine) propane sulphonic acid


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Nitrate uptake and reductase activities of the cyanobacterium Anabaena cycadeae and its mutant, lacking glutamine synthetase, (the glutamine auxotroph) were measured. The levels of both these enzymes were up to 25-fold higher in the mutant than in the parent (Anabaena cycadeae). The data indicate op