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Effect of benzimidazole on nicotinamide adenine dinucleotide phosphate phosphomonosterase activity in wheat leaves

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  • Chimica, Biochimica
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Summary

Nicotinamide adenine dinucleotide phosphate phosphomonoesterase was isolated and partially purified from wheat (Triticum aestivum L. var. Selkirk) leaves. The enzyme hadK NADP value of 1.4×10−4 M and a pH optimum of 5.9.In vitro activity of this enzyme was unaffected by precursors of NAD (nicotinamide and nicotinic acid) or cytokinis (kinetin and benzimidazole). However, when detached wheat leaves were treated with solutions of these compounds, the precursors lowered the specific activity while the cytokinins enhanced the activity. It is suggested that spatial separation and compartmentation of the enzyme and its substrate NADP account for the similar effect of benzimidazole on both.

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Author notes

  1. C. K. Chin

    Present address: , 3B-34 York Drive, 08817, Edison, New Jersey, USA

Authors and Affiliations

  1. Department of Botany, University of Manitoba, R3T 2N2), Winnipeg, Manitoba, (Canada

    H. R. Godavari, C. K. Chin & E. R. Waygood

Authors
  1. H. R. Godavari
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  2. C. K. Chin
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  3. E. R. Waygood
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Additional information

This work was supported by a grant No. A2698 from the National Research Council, Canada.

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Godavari, H.R., Chin, C.K. & Waygood, E.R. Effect of benzimidazole on nicotinamide adenine dinucleotide phosphate phosphomonosterase activity in wheat leaves. Experientia 32, 1140–1142 (1976). https://doi.org/10.1007/BF01927590

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