Abstract. Glutamate synthase is a multicomponent ironsulfur 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 32 Å. 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.
|Titolo:||Glutamate synthase: a fascinating pathway from L-glutamine to L-glutamate|
|Autori interni:||VANONI, MARIA ANTONIETTA (Penultimo)|
CURTI, BRUNO (Secondo)
|Parole Chiave:||Ammonia tunnel; Crystal structure; Electrospray ionization mass spectrometry; Glutamate synthase; Glutamine-dependent amidotransferase; Multicomponent enzyme; Substrate channeling|
|Settore Scientifico Disciplinare:||Settore BIO/10 - Biochimica|
|Data di pubblicazione:||2004|
|Digital Object Identifier (DOI):||10.1007/s00018-003-3316-0|
|Appare nelle tipologie:||01 - Articolo su periodico|
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