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Partial purification and characterization of a NADPH dependent tetrahydroalstonine synthase from Catharanthus roseus cell suspension cultures

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Abstract

A new enzyme was discovered which specifically hydrogenates the iminium form of cathenamine at position 21 to yield the heteroyohimbine alkaloid tetrahydroalstonine. The enzyme was partially purified (35-fold) from Catharanthus roseus cell suspension cultures. It was shown to use exclusively NADPH as reductant, the pH optimum is at 6.6, the temperature optimum at 30°C, the half life of the soluble enzyme preparation is 26 min at 37°C, and the molecular weight is 81 000 ± 3%. Evidence is presented for the occurrence of two distinct and different cathenamine reductases, one reducing the iminium form of this central intermediate to give tetrahydroalstonine, the other one reducing cathenamine to yield ajmalicine. Tetrahydroalstonine synthase was present in cell suspension cultures of C. ovalis, C. roseus, Picralima nitida, Rhazya stricta, and Vinca herbacea.

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Authors and Affiliations

  1. Lehrstuhl für Pharmazeutische Biologie, Universität München, Karlstrasse 29, D-8000, München 2, FRG

    T. Hemscheidt & M. H. Zenk

Authors
  1. T. Hemscheidt
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  2. M. H. Zenk
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Communicated by K. Hahlbrock

Dedicated to Prof. Dr. Franz Lingens on the occasion of his 60th birthday

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Hemscheidt, T., Zenk, M.H. Partial purification and characterization of a NADPH dependent tetrahydroalstonine synthase from Catharanthus roseus cell suspension cultures. Plant Cell Reports 4, 216–219 (1985). https://doi.org/10.1007/BF00269293

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  • DOI: https://doi.org/10.1007/BF00269293

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