Enzymes of ammonium assimilation inStreptomyces avermitilis |
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Authors: | J Novák E ?urdová V Jechová E Cimburková Z Vaněk |
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Institution: | (1) Laboratory of Biogenesis of Natural Metabolites, Institute of Microbiology, Czechoslovak Academy of Sciences, 142 20 Prague 4 |
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Abstract: | Glutamine synthetase (GS), glutamate synthase (GOGAT), glutamate dehydrogenase (GDH), alanine dehydrogenase (ADH) and alanine
aminotransferase (GPT) were detected in the cell-free homogenate ofStreptomyces avermitilis grown in a defined medium containing ammonium sulfate as the only nitrogen source. At an initial NH4
+ concentration of 7.5 mmol/L, high activities of GS, GOGAT and GDH were found while that of ADH was low. The ADH activity
was markedly increased at initially millimolar NH4
+ concentrations. In some characteristics of its NH4
+-assimilating system (e.g. control of some enzyme activities, the NADPH specificity of GOGAT, the presence of alanine aminotransferase),S. avermitilis differs from other known streptomycetes. |
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