Regulation of the activity of maize glutamate dehydrogenase by ammonium and potassium

Biosci Biotechnol Biochem. 2021 Feb 18;85(2):262-271. doi: 10.1093/bbb/zbaa020.

Abstract

Glutamate dehydrogenase (GDH) is an important enzyme in ammonium metabolism, the activity of which is regulated by multiple factors. In this study, we investigate the effects of ammonium and potassium on the activity of maize GDH. Our results show that both ammonium and potassium play multiple roles in regulating the activity of maize GDH, with the specific roles depending on the concentration of potassium. Together with the structural information of GDH, we propose models for the substrate inhibition of ammonium, and the elimination of substrate inhibition by potassium. These models are supported by the analysis of statistic thermodynamics. We also analyze the binding sites of ammonium and potassium on maize GDH, and the conformational changes of maize GDH. The findings provide insight into the regulation of maize GDH activity by ammonium and potassium and reveal the importance of the dose and ratio of nitrogen and potassium in crop cultivation.

Keywords: activity regulation; ammonium; glutamate dehydrogenase; potassium.

MeSH terms

  • Amino Acid Sequence
  • Ammonium Compounds / pharmacology*
  • Dose-Response Relationship, Drug
  • Glutamate Dehydrogenase / chemistry
  • Glutamate Dehydrogenase / metabolism*
  • Kinetics
  • Models, Molecular
  • Potassium / pharmacology*
  • Protein Conformation
  • Zea mays / enzymology*

Substances

  • Ammonium Compounds
  • Glutamate Dehydrogenase
  • Potassium