Data di Pubblicazione:
2004
Citazione:
Glutamate synthase: a fascinating pathway from L-glutamine to L-glutamate / R..H..H. van den Heuvel, B. Curti, M.A. Vanoni, A. Mattevi. - In: CELLULAR AND MOLECULAR LIFE SCIENCES. - ISSN 1420-682X. - 61:6(2004), pp. 669-681.
Abstract:
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.
Tipologia IRIS:
01 - Articolo su periodico
Keywords:
Ammonia tunnel; Crystal structure; Electrospray ionization mass spectrometry; Glutamate synthase; Glutamine-dependent amidotransferase; Multicomponent enzyme; Substrate channeling
Elenco autori:
R..H..H. van den Heuvel, B. Curti, M.A. Vanoni, A. Mattevi
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