z-logo
open-access-imgOpen Access
Enzyme redundancy and the importance of 2‐oxoglutarate in plant ammonium assimilation
Author(s) -
Michael Hodges
Publication year - 2002
Publication title -
journal of experimental botany
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.616
H-Index - 242
eISSN - 1460-2431
pISSN - 0022-0957
DOI - 10.1093/jexbot/53.370.905
Subject(s) - assimilation (phonology) , nitrogen assimilation , ammonium , biochemistry , enzyme , biology , photorespiration , metabolic pathway , amino acid , nitrogen , ammonia , metabolism , chemistry , organic chemistry , philosophy , linguistics
Ammonium is the reduced nitrogen form available to plants for assimilation into amino acids. This is achieved by the GS/GOGAT pathway that requires carbon skeletons in the form of 2-oxoglutarate. To date, the exact enzymatic origin of this organic acid for plant ammonium assimilation is unknown. Isocitrate dehydrogenases and aspartate aminotransferases have been proposed to carry out this function. Since different (iso)forms located in several subcellular compartments are present within a plant cell, recent efforts have concentrated on evaluating the involvement of these enzymes in ammonium assimilation. Furthermore, several observations indicate that 2-oxoglutarate is a good candidate as a metabolic signal to regulate the co-ordination of C and N metabolism. This will be discussed with respect to recent advances in bacterial signalling processes involving a 2-oxoglutarate binding protein called PII.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom