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Ammonia assimilation and glutamate incorporation in coenzyme F420 derivatives of Methanosarcina barkeri.
- Source :
-
Antonie van Leeuwenhoek [Antonie Van Leeuwenhoek] 1991 May; Vol. 59 (4), pp. 243-8. - Publication Year :
- 1991
-
Abstract
- Methanosarcina barkeri was able to grow on L-alanine and L-glutamate as sole nitrogen sources. Cell yields were 0.5 g/l and 0.7 g/l (wet wt), respectively. The mechanism of ammonia assimilation in Methanosarcina barkeri strain MS was studied by analysis of enzyme activities. Activity levels of nitrogen-assimilating enzymes in extracts of cells grown on different nitrogen sources (ammonia, 0.05-100 mM; L-alanine, 10 mM; L-glutamate, 10 mM) were compared. Activities of glutamate dehydrogenase, glutamate synthase, glutamine synthetase, glutamate oxaloacetate transaminase and glutamate pyruvate transaminase could be measured in cells grown on these three nitrogen sources. Alanine dehydrogenase was not detected under the growth conditions used. None of the measured enzyme activities varied significantly in response to the NH4+ concentration. The length of the poly-gamma-glutamyl side chain of F420 derivatives turned out to be independent of the concentration of ammonia in the culture medium.
- Subjects :
- Alanine Transaminase metabolism
Aspartate Aminotransferases metabolism
Cell Division
Chromatography, High Pressure Liquid
Culture Media
Euryarchaeota enzymology
Euryarchaeota growth & development
Glutamate Dehydrogenase metabolism
Glutamate Synthase metabolism
Glutamate-Ammonia Ligase metabolism
Glutamic Acid
Nitrogen
Riboflavin metabolism
Alanine metabolism
Ammonia metabolism
Euryarchaeota metabolism
Glutamates metabolism
Riboflavin analogs & derivatives
Subjects
Details
- Language :
- English
- ISSN :
- 0003-6072
- Volume :
- 59
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- Antonie van Leeuwenhoek
- Publication Type :
- Academic Journal
- Accession number :
- 1679322
- Full Text :
- https://doi.org/10.1007/BF00583677