Ammonium Assimilation


Determination of Essentiality
Nitrogen Metabolism and Nitrogenous Constituents in Plants
  Nitrate Assimilation
    - Nitrate Reductase
    - Nitrite Reductase
  Ammonium Assimilation
    - Glutamine Synthetase
    - Glutamate Synthase
    - Glutamic Acid Dehydrogenase
    - Transamination
    - Amidation
  Proteins and Other Nitrogenous Compounds
Diagnosis of Nitrogen Status in Plants
  Symptoms of Deficiency and Excess
  Concentrations of Nitrogen in Plants
    - Concentrations of Nitrogen in Plant Parts
    - Ratios of Concentrations of Nitrogen to Other Nutrients in Plants
Nitrogen in Soils
  Forms of Nitrogen in Soils
    - Organic Nitrogen in Soil
    - Inorganic Nitrogen in Soil
Soil Testing for Nitrogen
  Determinations of Total Nitrogen
  Biological Determinations of Availability Indexes
    - Determination of Inorganic Nitrogen
      - Ammonium
      - Nitrate
      - Amino Sugars
Nitrogen Fertilizers
  Properties and Use of Nitrogen Fertilizers
    - Anhydrous Ammonia: 82% N
    - Aqua Ammonia: 21% N
    - Urea: 46% N
    - Ammonium Nitrate: 34% N
    - Ammonium Sulfate: 21% N
    - Nitrogen Solutions: 28–32% N
    - Ammonium Phosphates: 10–21% N
    - Other Inorganic Nitrogen Fertilizers
    - Organic Nitrogen Fertilizers: 0.2–15% N
The metabolism of ammonium into amino acids and amides is the main mechanism of assimilation and detoxification of ammonium. Glutamic acid formation is a port of entry of nitrogen into organic compounds and occurs in the chloroplasts or mitochondria. Ammonium assimilation in root mitochondria probably uses ammonium absorbed in high concentrations from nutrient solutions. One enzyme is involved in ammonium assimilation in mitochondria: glutamic acid dehydrogenase. Ammonium assimilation in chloroplasts utilizes the ammonium that is formed from the reduction of nitrite by nitrite reductase and that which is released in photorespiration. Two enzymes are involved in chloroplasts, glutamine synthetase and glutamate synthase. Glutamine synthetase forms glutamine from ammonium and glutamate (glutamic acid).

Glutamate synthase forms glutamate from glutamine and α-oxoglutarate (α-ketoglutaric acid). These enzymes are also active in roots and nodules (N2 fixation). These enzymes assimilate most of the ammonium derived from absorption from dilute solutions, reduction of nitrate, N2 fixation, or photorespiration (18–25). Further discussions of glutamine synthetase, glutamate synthase, and glutamic acid dehydrogenase follow.

Glutamine Synthetase

Ammonium + glutamate + ATP + reduced ferredoxin → glutamine + oxidized ferredoxin

Glutamate Synthase

Glutamine + α-oxoglutarate → 2 glutamate

Sum (or net): Ammonium + α-oxoglutarate + ATP + reduced ferredoxin → glutamate + oxidized ferredoxin Glutamine synthetase has a high affinity for ammonium and thus can assimilate ammonium at low concentrations, such as those that occur from the reduction of nitrate. If this enzyme is inhibited, however, ammonium may accumulate to phytotoxic levels. Ammonium accumulation to toxic levels from the inhibition of glutamine synthetase is the mode of action of the herbicide glufosinate ammonium (26,27).

Glutamic Acid Dehydrogenase

Ammonium + α-oxoglutarate + ATP + reduced pyridine nucleotide (NADH, NADPH) → glutamate + oxidized pyridine nucleotide (NAD+, NADP+)

Another pathway for ammonium assimilation into organic compounds is by glutamic acid dehydrogenase, which is located in the mitochondria (28). Glutamic acid dehydrogenase has a low affinity for ammonium and becomes important in ammonium assimilation at high concentrations of ammonium and at low pH in growth media (15).


Glutamate + α-oxyacid → α-oxoglutarate + α-amino acid

Ammonium that is assimilated into glutamate from mitochondrial or chloroplastic assimilation can be transferred by aminotransferases (transaminases) to an appropriate α-oxyacid (α- ketoacid) to form an α-amino acid. The transfer can also be to other keto-groups on carbon chains to form, for example, λ- or δ-amino acids. The keto acids for the synthesis of amino acids are derived from photosynthesis, glycolysis, and the tricarboxylic acid cycle, among other processes.


Glutamate + ammonium + ATP → glutamine + ADP

Amides are formed by the amidation of carboxyl groups. Amides are nitrogen-rich compounds that can store or transport nitrogen. Common amides are glutamine (5C, 2N) and asparagine (4C, 2N). Glutamine is formed from amidation of glutamic acid (glutamate), and asparagine is formed by amidation of aspartic acid (aspartate). Often, when the external supply of ammonium is high, asparagine, a metabolite unique to plants, will dominate among the amides, as plants respond to conserve carbon in the detoxification of ammonium.