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Purification and characterization of the NADP-dependent glutamate dehydrogenase from Bacillus fastidiosus

Antonie van Leeuwenhoek volume 55, pages 303–311 (1989)Cite this article

Abstract

Ammonia assimilation in Bacillus fastidiosus proceeds via the NADP-dependent glutamate dehydrogenase. The enzyme, purified to homogeneity, is composed of identical subunits with a molecular weight of about 48 000 dalton. Presumably the enzyme is a hexamer. The enzyme is specific for NADP (H). The pH optima for the amination and deamination reactions are 7.7 and 8.6, respectively. The temperature optimum is 60°C. Furthermore, temperature stability and apparent Km values for substrates of both the amination and deamination reactions were determined. Several metabolites were tested for their effect on the enzyme activity. Only malate and fumarate showed some inhibitory effect.

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Abbreviations

GDH:

glutamate dehydrogenase

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Affiliations

  1. Department of Microbiology, Faculty of Science, University of Nijmegen, Toernooiveld, NL-6525 ED, Nijmegen, The Netherlands

    H. J. M. Op Den Camp, K. D. Liem, P. Meesters, J. M. H. Hermans & C. Van Der Drift

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  1. H. J. M. Op Den Camp
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  2. K. D. Liem
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  3. P. Meesters
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  4. J. M. H. Hermans
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  5. C. Van Der Drift
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Op Den Camp, H.J.M., Liem, K.D., Meesters, P. et al. Purification and characterization of the NADP-dependent glutamate dehydrogenase from Bacillus fastidiosus . Antonie van Leeuwenhoek 55, 303–311 (1989). https://doi.org/10.1007/BF00398509

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  • DOI: https://doi.org/10.1007/BF00398509

Key words

  • Bacillus fastidiosus
  • glutamate dehydrogenase
  • nitrogen metabolism