Expression and functional analysis of glutamate synthase small subunit-like proteins from archaeon Pyrococcus horikoshii

Dincturk H. B., Cunin R., Akce H.

MICROBIOLOGICAL RESEARCH, vol.166, no.4, pp.294-303, 2011 (SCI-Expanded) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 166 Issue: 4
  • Publication Date: 2011
  • Doi Number: 10.1016/j.micres.2010.03.006
  • Journal Name: MICROBIOLOGICAL RESEARCH
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.294-303
  • Istanbul Technical University Affiliated: Yes

Abstract

Glutamate synthase, glutamine a-ketoglutarate amidotransferase (often abbreviated as GOGAT) is a key enzyme in the early stages of ammonia assimilation in bacteria, algae and plants, catalyzing the reductive transamidation of the amido nitrogen from glutamine to a-ketoglutarate to form two molecules of glutamate. Most bacterial glutamate synthases consist of a large and small subunit. The genomes of three Pyrococcus species harbour several open reading frames which show homology with the small subunit of glutamate synthase. There are no open reading frames which may be coding for a large subunit responsible for the glutamate formation in these pyrococcal genomes.