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Glutamine synthetase and arginine inhibition of nitrate reductase activity inAnabaena cycadeae

✍ Scribed by S. Singh; P. S. Bisen

Publisher
Springer
Year
1994
Tongue
English
Weight
189 KB
Volume
10
Category
Article
ISSN
1573-0972

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✦ Synopsis

Wild-type Anabaena cycadeae with normal glutamine synthetase (GS) activity utilized arginine as sole N source whereas a mutant strain lacking GS activity did not. Nitrate reductase (NR) activity, higher in the mutant strain than the wild-type strain, was inhibited by arginine though arginine-dependent NH + generation was higher in the mutant strain than in the wild-type. This suggests that (1) NR activity is NO~--inducible and argininerepressible; and (2) while GS activity is required for the assimilation of arginine as sole N-source, it is not required for arginine inhibition of NR activity.

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