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- Title
Glutamate synthase: a fascinating pathway from L-glutamine to L-glutamate.
- Authors
van den Heuvel, R H H; Curti, B; Vanoni, M A; Mattevi, A
- 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 32A. 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.
- Publication
Cellular and molecular life sciences : CMLS, 2004, Vol 61, Issue 6, p669
- ISSN
1420-682X
- Publication type
Journal Article
- DOI
10.1007/s00018-003-3316-0