Abstract
Glutamate synthase is a multicomponent iron-sulfur flavoprotein belonging to the class of N-terminal nucleophile amidotransferases. It catalyzes the conversion of L-glutamine and 2-oxoglutarate into two molecules of L-glutamate. In recent years the X-ray structures of the ferredoxin-dependent glutamate synthase and of the a subunit of the NADPH-dependent glutamate synthase have become available. Thanks to X-ray crystallography, it is now known that the ammonia reaction intermediate is transferred via an intramolecular tunnel from the amidotransferase domain to the synthase domain over a distance of about 32Å. Although ammonia channeling is a recurrent theme for N-terminal nucleophile and triad-type amidotransferases, the molecular mechanisms of ammonia transfer and its control are different for each known amidotransferase. This review focuses on the intriguing mechanism of action and self-regulation of glutamate synthase with a special focus on the structural data.
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Received 8 August 2003; received after revision 15 September 2003; accepted 17 September 2003
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van den Heuvel, R.H.H., Curti, B., Vanoni, M.A. et al. Glutamate synthase: a fascinating pathway from L-glutamine to L-glutamate. CMLS, Cell. Mol. Life Sci. 61, 669–681 (2004). https://doi.org/10.1007/s00018-003-3316-0
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DOI: https://doi.org/10.1007/s00018-003-3316-0