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Plant Cell Physiol. 2016 Apr;57(4):675-89. doi: 10.1093/pcp/pcv184. Epub 2015 Dec 1.

Asparagine Metabolic Pathways in Arabidopsis.

Author information

1
INRA, IJPB, UMR1318, ERL CNRS 3559, Saclay Plant Sciences, RD10, F-78026 Versailles, France.
2
University of Guelph, Department of Molecular and Cellular Biology, Guelph, Ontario, Canada N1G 2W1.
3
INRA, IJPB, UMR1318, ERL CNRS 3559, Saclay Plant Sciences, RD10, F-78026 Versailles, France Akira.Suzuki@versailles.inra.fr.

Abstract

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.

KEYWORDS:

Amides and amino acids; Ammonium assimilation; Arabidopsis; Asparagine synthesis and catabolism; Nitrogen metabolism; Transport

PMID:
26628609
DOI:
10.1093/pcp/pcv184
[Indexed for MEDLINE]

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