{"refrec":{"BRefID":280751,"RR":"<b>Dincturk, H.B.; Cunin, R.; Akce, H.</b> (2011). Expression and functional analysis of glutamate synthase small subunit-like proteins from archaeon <i>Pyrococcus horikoshii</i>. <i>Microbiological Research 166(4)</i>: 294-303. <a href=\"http://dx.doi.org/10.1016/j.micres.2010.03.006\" target=\"_blank\">dx.doi.org/10.1016/j.micres.2010.03.006</a>","BEntID":272770,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":null,"RefStringPartII":". <i>Microbiological Research 166(4)</i>: 294-303. <a href=\"https://dx.doi.org/10.1016/j.micres.2010.03.006\" target=\"_blank\">https://dx.doi.org/10.1016/j.micres.2010.03.006</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Dincturk, H.B.; Cunin, R.; Akce, H.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Dincturk, H.B. <i>et al.</i>","Englishabstract":"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 <i>Pyrococcus</i> 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 <i>P</i>. <i>horikoshii</i> were cloned and expressed in <i>Escherichia coli</i> 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.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"Expression and functional analysis of glutamate synthase small subunit-like proteins from archaeon <i>Pyrococcus horikoshii</i>","OrigTitleLangCode":"en","OrigTitleLangCodeExtended":"eng","OrigTitleLangID":15,"DateLastModified":{"date":"2024-12-10 01:33:17.368041","timezone_type":1,"timezone":"+01:00"},"UserAccessRight":null,"UserAccID":null,"AuthorKeywords":"Glutamate synthase; Pyroccoccus horikoshii; Thermophilic oxidoreductase;Gene duplication; Horizontal gene transfer","OtherDescriptors":null,"Notes":null,"AnaPub":2011,"MonPub":null,"DateUpdate":"2016-10-20","DateCreate":"2016-10-09","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000291451300005","VABBcode":null,"OpenAcc":0,"DOI":"10.1016/j.micres.2010.03.006"},"refs":null,"anarec":{"AnaID":280751,"PubliDate":2011,"Pagination":"294-303","XtraPublOfAnaID":null,"ISBN":null,"Volume":"166","Issue":"4","BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":274722,"SerRR":"Microbiological Research: Jena.  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