, Volume 168, Issue 3, pp 316–323

Carbon and nitrogen metabolism in barley (Hordeum vulgare L.) mutants lacking ferredoxin-dependent glutamate synthase

  • A. C. Kendall
  • R. M. Wallsgrove
  • N. P. Hall
  • J. C. Turner
  • P. J. Lea


Five mutant lines of barley (Hordeum vulgare L.), which are only able to grow at elevated levels of CO2, contain less than 5% of the wild-type activity of ferredoxin-dependent glutamate synthase (EC Two of these lines (RPr 82/1 and RPr 82/9) have been studied in detail. Leaves and roots of both lines contain normal activities of NADH-dependent glutamate synthase (EC and the other enzymes of ammonia assimilation. Under conditions that minimise photorespiration, both mutants fix CO2 at normal rates; on transfer to air, the rates drop rapidly to 15% of the wild-type. Incorporation of 14CO2 into sugar phosphates and glycollate is increased under such conditions, whilst incorporation of radioactivity into serine, glycine, glycerate and sucrose is decreased; continuous exposure to air leads to an accumulation of 14C in malate. The concentrations of malate, glutamine, asparagine and ammonia are all high in air, whilst aspartate, alanine, glutamate, glycine and serine are low, by comparison with the wild-type parent line (cv. Maris Mink), under the same conditions. The metabolism of [14C]glutamate and [14C]glutamine by leaves of the mutants indicates a very much reduced ability to convert glutamine to glutamate. Genetic analysis has shown that the mutation in RPr 82/9 segregates as a single recessive nuclear gene.

Key words

Ammonia/ammonium metabolism Glutamate synthase (ferredoxin dependent) Hordeum (mutant) Mutant (barley) Photorespiration 



glutamate dehydrogenase (EC


glutamine synthetase (EC


ribulose 1,5-bisphosphate


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Copyright information

© Springer-Verlag 1986

Authors and Affiliations

  • A. C. Kendall
    • 1
  • R. M. Wallsgrove
    • 1
  • N. P. Hall
    • 1
  • J. C. Turner
    • 1
  • P. J. Lea
    • 1
  1. 1.Department of BiochemistryRothamsted Experimental StationHarpendenUK
  2. 2.Department of Biological SciencesUniversity of LancasterUK

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