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Cellular and Molecular Life Sciences CMLS

, Volume 55, Issue 4, pp 617–638 | Cite as

Glutamate synthase: a complex iron-sulfur flavoprotein

  • M. A. Vanoni
  • B. Curti

Abstract.

Glutamate synthase is a complex iron-sulfur flavoprotein that forms l-glutamate from l-glutamine and 2-oxoglutarate. It participates with glutamine synthetase in ammonia assimilation processes. The known structural and biochemical properties of glutamate synthase from Azospirillum brasilense, a nitrogen-fixing bacterium, will be discussed in comparison to those of the ferredoxin-dependent enzyme from photosynthetic tissues and of the eukaryotic reduced pyridine nucleotide-dependent form of glutamate synthase in order to gain insight into the mechanism of the glutamate synthase reaction. Sequence analyses also revealed that the small subunit of bacterial glutamate synthase may be the prototype of a novel class of flavin adenine dinucleotide- and iron-sulfur-containing oxidoreductase widely used as an enzyme subunit or domain to transfer reducing equivalents from NAD(P)H to an acceptor protein or protein domain.

Key words. Glutamate synthase; flavoprotein; iron-sulfur clusters; ammonia assimilation; nitrogen metabolism; oxidoreductases; amidotransferases; electron transfer. 

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Copyright information

© Birkhäuser Verlag Basel, 1999

Authors and Affiliations

  • M. A. Vanoni
    • 1
  • B. Curti
    • 1
  1. 1.Dipartimento di Fisiologia e Biochimica Generali, Università degli Studi di Milano, Via Celoria 26, I-20133 Milano (Italy), Fax +39 22362451, e-mail: curti@unimi.it, mav@unimi.itIT

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