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The isoenzyme seven of tobacco NAD(H)- dependent glutamate dehydrogenase exhibits high deaminating and low aminatingactivities in vivo

Paranychianakis Nikolaos, Damianos S. Skopelitis, Antonios Kouvarakis, Apostolis Spyros, Kalliopi A. Roubelakis-Angelakis

Απλή Εγγραφή


URIhttp://purl.tuc.gr/dl/dias/1F7862E7-6408-4140-923D-A7BF35A23260-
Αναγνωριστικόhttps://doi.org/10.1104/pp.107.107813-
Γλώσσαen-
ΤίτλοςThe isoenzyme seven of tobacco NAD(H)- dependent glutamate dehydrogenase exhibits high deaminating and low aminating activities in vivoen
ΔημιουργόςParanychianakis Nikolaosen
ΔημιουργόςΠαρανυχιανακης Νικολαοςel
ΔημιουργόςDamianos S. Skopelitisen
ΔημιουργόςAntonios Kouvarakisen
Δημιουργός Apostolis Spyrosen
Δημιουργός Kalliopi A. Roubelakis-Angelakisen
Δημιουργός Euripides G. Stephanouen
ΕκδότηςAmerican Society of Plant Biologistsen
ΠερίληψηFollowing the discovery of glutamine synthetase/glutamate (Glu) synthase, the physiological roles of Glu dehydrogenase (GDH) in nitrogen metabolism in plants remain obscure and is the subject of considerable controversy. Recently, transgenics were used to overexpress the gene encoding for the β-subunit polypeptide of GDH, resulting in the GDH-isoenzyme 1 deaminating in vivo Glu. In this work, we present transgenic tobacco (Nicotiana tabacum) plants overexpressing the plant gdh gene encoding for the α-subunit polypeptide of GDH. The levels of transcript correlated well with the levels of total GDH protein, the α-subunit polypeptide, and the abundance of GDH-anionic isoenzymes. Assays of transgenic plant extracts revealed high in vitro aminating and low deaminating activities. However, gas chromatography/mass spectrometry analysis of the metabolic fate of 15NH4 or [15N]Glu revealed that GDH-isoenzyme 7 mostly deaminates Glu and also exhibits low ammonium assimilating activity. These and previous results firmly establish the direction of the reactions catalyzed by the anionic and cationic isoenzymes of GDH in vivo under normal growth conditions and reveal a paradox between the in vitro and in vivo enzyme activities.el
ΤύποςPeer-Reviewed Journal Publicationen
ΤύποςΔημοσίευση σε Περιοδικό με Κριτέςel
Άδεια Χρήσηςhttp://creativecommons.org/licenses/by/4.0/en
Ημερομηνία2015-10-23-
Ημερομηνία Δημοσίευσης2015-
Βιβλιογραφική Αναφορά. Skopelitis, D.S., Paranychianakis, N.V., Spyros, A., Kouvarakis, A., Stephanou, E., Roubelakis-Angelakis, K.A., "The isoenzyme seven of tobacco NAD(H)- dependent glutamate dehydrogenase exhibits high deaminating and low aminating activities in vivo", Plant Physiology, Vol. 145, no. 4, pp. 1726-1734, Dec. 2007, doi: 10.1104/pp.107.107813en

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