Abstract
There is increasing evidence that the assimilation of ammonia by N2 fixing organisms proceeds by way of the dual enzyme system of gfutamine synthetase (GS) (EC. 6.3.1.2 — Equation 1) and glutamate synthase (GOGAT) (EC. 2.6.1.53 — Equation 2) (34, 12). Glutamate synthase was originally isolated by Tempst et al., (66) from ammonia-limited chemostat cultures of Klebsiella aerogenes. This discovery provided an alternative pathway for the assimilation of ammonia other than the reductive amination of 2-oxoglutarate, catalysed by glutamate dehydrogenase (GDH) (EC. 1.4. 1.3., Equation 3). Although the GS/GOGAT pathway proceeds at the expense of an extra ATP, the greater affinity of GS and GOGAT for their substrates compared to glutamate dehydrogenase would suggest that the GS/GOGAT system is the major route for ammonia assimilation in microorganisms under conditions of limiting ammonia (33, 67, 7, 12). This pathway has also been demonstrated in higher plants (17, 13, 26).
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Scott, D.B. (1978). Ammonia Assimilation in N2-Fixing Systems. In: Döbereiner, J., Burris, R.H., Hollaender, A., Franco, A.A., Neyra, C.A., Scott, D.B. (eds) Limitations and Potentials for Biological Nitrogen Fixation in the Tropics. Basic Life Sciences, vol 10. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-8957-0_16
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