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Derepression of nitrate reductase fromDerxia gummosaand some properties of the purified enzyme

โœ Scribed by Rongchen Wang; D. J. D. Nicholas

Publisher
Springer
Year
1986
Tongue
English
Weight
952 KB
Volume
145
Category
Article
ISSN
0302-8933

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โœฆ Synopsis

The assimilatory NADH-nitrate reductase has been purified to electrophoretic homogeneity from the Nzfixing bacterium Derxia gummosa. This enzyme has a molecular weight of ~ 175 kdaltons and is composed of two dissimilar subunits (88 and 80 kdaltons, respectively). Typical cytochrome b557 spectra were observed for the purified enzyme, reduced with sodium dithionite.

Both ammonia and glutamine inhibited the induction of nitrate reductase in washed cells from cultures grown with NH4C1. The inhibition by ammonia, but not that by glutamine was relieved by methionine sulphoximine. The induction of nitrate reductase was also inhibited by azaserine. In cells treated with methionine sulphoximine, glutamine content was decreased whereas it increased in those treated with azaserine. The synthesis of RNA during the derepression of nitrate reductase was also inhibited by glutamine. Thus glutamine is involved in regulating the derepression of nitrate reductase at the transcription level.

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