Zoeken
Zoeken kan via de modus 'eenvoudig zoeken' (één veld) of uitgebreid via 'geavanceerd zoeken' (meerdere velden). Zo kan je bv. zoeken op een combinatie van een auteursnaam (auteur), een jaartal (jaar) en een documenttype.
Boekenmand
Nuttige resultaten kan je aanvinken en toevoegen aan een mandje. De inhoud hiervan kan je exporteren of afdrukken (naar bv. PDF).
RSS
Op de hoogte blijven van nieuw toegevoegde publicaties binnen uw interessegebied? Dit kan door een RSS-feed (?) te maken van jouw zoekopdracht.
nieuwe zoekopdracht
Expression and functional analysis of glutamate synthase small subunit-like proteins from archaeon Pyrococcus horikoshii
Dincturk, H.B.; Cunin, R.; Akce, H. (2011). Expression and functional analysis of glutamate synthase small subunit-like proteins from archaeon Pyrococcus horikoshii. Microbiological Research 166(4): 294-303. dx.doi.org/10.1016/j.micres.2010.03.006
In: Microbiological Research: Jena. ISSN 0944-5013
|  |
| Trefwoorden |
Pyrococcus horikoshii Gonzalez, Masuchi, Robb, Ammerman, Maeder, Yanagibayashi, Tamaoka & Kato, 1998 [WoRMS]
Marien/Kust |
| Author keywords |
Glutamate synthase; Pyroccoccus horikoshii; Thermophilic oxidoreductase;Gene duplication; Horizontal gene transfer |
| Auteurs | | Top |
- Dincturk, H.B.
- Cunin, R.
- Akce, H.
|
|
|
| Abstract |
Glutamate synthase, glutamine α-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 α-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.In this work, two open reading frames PH0876 and PH1873 from P. horikoshii were cloned and expressed in Escherichia coli as soluble proteins. Both proteins show NADPH-dependent oxidoreductase activity using artificial electron acceptors iodonitrotetrazolium chloride at thermophilic conditions. It is possible that these open reading frames are the products of gene duplication and that they are the early forms of an electron transfer domain in archaea which may have later contributed to many electron transfer enzymes. |
IMIS is ontwikkeld en wordt gehost door het VLIZ.
