Asparagine metabolic pathways in arabidopsis

Autor: Akira Suzuki, Laure Gaufichon, Steven J. Rothstein
Přispěvatelé: Institut Jean-Pierre Bourgin (IJPB), Institut National de la Recherche Agronomique (INRA)-AgroParisTech, Department of Molecular and Cellular Biology, University of Guelph
Jazyk: angličtina
Rok vydání: 2016
Předmět:
Zdroj: Plant and Cell Physiology
Plant and Cell Physiology, Oxford University Press (OUP), 2016, 57 (4), pp.675-689. ⟨10.1093/pcp/pcv184⟩
ISSN: 0032-0781
1471-9053
Popis: Inorganic nitrogen in the form of ammonium is assimilated into asparagine via multiple steps involving glutamine synthetase (GS), glutamate synthase (GOGAT), aspartate aminotransferase (AspAT) and asparagine synthetase (AS) in Arabidopsis. The asparagine amide group is liberated by the reaction catalyzed by asparaginase (ASPG) and also the amino group of asparagine is released by asparagine aminotransferase (AsnAT) for use in the biosynthesis of amino acids. Asparagine plays a primary role in nitrogen recycling, storage and transport in developing and germinating seeds, as well as in vegetative and senescence organs. A small multigene family encodes isoenzymes of each step of asparagine metabolism in Arabidopsis, except for asparagine aminotransferase encoded by a single gene. The aim of this study is to highlight the structure of the genes and encoded enzyme proteins involved in asparagine metabolic pathways; the regulation and role of different isogenes; and kinetic and physiological properties of encoded enzymes in different tissues and developmental stages.
Databáze: OpenAIRE