Published October 31, 2021 | Version v1

Petroselinum crispum subsp. root SDH

  • 1. Department of Biochemistry, Faculty of Science, Charles University, Hlavova 2030, Prague 2, 128 40, Czech Republic
  • 2. Department of Biochemistry, Faculty of Science, Charles University, Hlavova 2030, Prague 2, 128 40, Czech Republic & Tomas Bata University in Zlín, Faculty of Technology, Department of Physics and Materials Engineering, N´am. T. G. Masaryka 5555, 760 01, Zlín, Czech Republic & Tomas Bata University in Zlín, Faculty of Technology, Department of Physics and Materials Engineering, N´am. T. G. Masaryka 5555, 760 01, Zlín, Czech Republic

Description

3.1. P. crispum root extracts show high SDH activity

One of the reasons why SDH activity is low in plant crude extracts is the presence of phenolics. In general, when exposed to air, plant phenolics are readily oxidized, generating products that form complexes with proteins and inhibit enzyme activity (Buchanan et al., 2000), as shown in Fig. A.1. Since the total phenolic content is very high in plants, especially in medicinal herbs (Tupec et al., 2017), a group of vegetables was chosen to identify a source of high SDH activity from non-photosynthetic tissue. From the group of 8 vegetable sources, the P. crispum root exhibited the highest SDH activity. After 3-step purification procedure specific SDH activity in P. crispum was 470 nmol. min-1. mg -1. This activity was lower than SDH from recombinant sources e.g. (Tahara et al., 2021) but comparable with SDH from etiolated pea epicotyls (Balinsky and Davies, 1961), or tomato (Solanum lycopersicum L.) fruit (Lourenco and Neves, 1984) or Cucumis sativus L. pulp (Lourenco et al., 1991).

Notes

Published as part of Hýskova, Veronika, Belonozníkov, Katerina, Smeringaiova, Ingrida, Kavan, Daniel, Ingr, Marek & Ryslava, Helena, 2021, How is the activity of shikimate dehydrogenase from the root of Petroselinum crispum (parsley) regulated and which side reactions are catalyzed?, pp. 1-12 in Phytochemistry (112881) (112881) 190 on page 6, DOI: 10.1016/j.phytochem.2021.112881, http://zenodo.org/record/8270251

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Additional details

Biodiversity

Scientific name authorship
SDH
Kingdom
Plantae
Phylum
Tracheophyta
Order
Apiales
Family
Apiaceae
Genus
Petroselinum
Species
crispum
Taxon rank
species

References

  • Buchanan, B. B., Gruissem, W., Jones, R. L., 2000. Biochemistry & Molecular Biology of Plants. American Society of Plant Physiologists, Rockville, Maryland.
  • Tupec, M., Hyskova, V., Belonoznikova, K., Hranicek, J., Cerveny, V., Ryslava, H., 2017. Characterization of some potential medicinal plants from Central Europe by their antioxidant capacity and the presence of metal elements. Food Biosci 20, 43 - 50. https: // doi. org / 10.1016 / j. fbio. 2017.08.001.
  • Tahara, K., Nishiguchi, M., Funke, E., Miyazawa, S. - I., Miyama, T., Milkowski, C., 2021. Dehydroquinate dehydratase / shikimate dehydrogenases involved in gallate biosynthesis of the aluminum-tolerant tree species Eucalyptus camaldulensis. Planta 253. https: // doi. org / 10.1007 / s 00425 - 020 - 03516 - w.
  • Balinsky, D., Davies, D. D., 1961. Aromatic biosynthesis in higher plants. 1. Preparation and properties of dehydroshikimic reductase. Biochem. J. 80, 292 - 296. https: // doi. org / 10.1042 / bj 0800292.
  • Lourenco, E. J., Neves, V. A., 1984. Partial purification and some properties of shikimate dehydrogenase from tomatoes. Phytochemistry 23, 497 - 499. https: // doi. org / 10.1016 / S 0031 - 9422 (00) 80366 - 0.
  • Lourenco, E. J., Silva, G. M., Neves, V. A., 1991. Purification and properties of shikimate dehydrogenase from cucumber (Cucumis sativus L.). J. Agric. Food Chem. 39, 458 - 462. https: // doi. org / 10.1021 / jf 00003 a 006.