Skip to main content
PMC home page
Plant Physiology logoLink to Plant Physiology
. 1982 Sep;70(3):745–748. doi: 10.1104/pp.70.3.745

Distribution of Secondary Plant Metabolites and Their Biosynthetic Enzymes in Pea (Pisum sativum L.) Leaves 1

Anthocyanins and Flavonol Glycosides

Geza Hrazdina 1,2,3, Gerald A Marx 1,2,3, Harvey C Hoch 1,2,3
PMCID: PMC1065763  PMID: 16662568

Abstract

Leaves of a novel strain of peas (Pisum sativum L.) were used to determine the distribution of secondary metabolites and their biosynthetic enzymes. Leaf epidermal layers in this strain are easily separated from the parenchyma. Anthocyanins and flavonol glycosides were localized in epidermal vacuoles only. Among the biosynthetic enzymes studied, phenylalanine ammonia-lyase (PAL, EC 4.3.1.5), S-adenosyl-1-methionine (SAM):caffeic acid and SAM:quercetin methyltransferases (o-dihydric phenol methyltransferase, EC 2.1.1.42) and a flavonoid 7-O-glucosyltransferase (EC 2.4.1.91) were chiefly localized in the parenchyma, whereas trans-cinnamate 4-monooxygenase (EC 1.14.13.11), hydroxycinnamate:CoA ligases (EC 6.2.1.12) and a flavonoid 3-O-glucosyltransferase (EC 2.4.1.91) were found mainly in the epidermis. Flavanone (chalcone) synthase activity was found only in the epidermis, whereas chalcone isomerase (EC 5.5.1.6) was evenly distributed in epidermal and parenchyma tissues.

Full text

PDF
747

Images in this article

746Fig. 1
on p.746

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Hahlbrock K., Ebel J., Ortmann R., Sutter A., Wellmann E., Grisebach H. Regulation of enzyme activities related to the biosynthesis of flavone glycosides in cell suspension cultures of parsley (Petroselinum hortense). Biochim Biophys Acta. 1971 Jul 20;244(1):7–15. doi: 10.1016/0304-4165(71)90114-0. [DOI] [PubMed] [Google Scholar]
  2. Hrazdina G., Kreuzaler F., Hahlbrock K., Grisebach H. Substrate specificity of flavanone synthase from cell suspension cultures of parsley and structure of release products in vitro. Arch Biochem Biophys. 1976 Aug;175(2):392–399. doi: 10.1016/0003-9861(76)90526-9. [DOI] [PubMed] [Google Scholar]
  3. Knobloch K. H., Hahlbrock K. Isoenzymes of p-coumarate: CoA ligase from cell suspension cultures of Glycine max. Eur J Biochem. 1975 Mar 17;52(2):311–320. doi: 10.1111/j.1432-1033.1975.tb03999.x. [DOI] [PubMed] [Google Scholar]
  4. Oettmeier W., Heupel A. Identification of flavonoids and cinnamic acid derivatives from spinach chloroplast preparations. Z Naturforsch B. 1972 Feb;27(2):177–183. doi: 10.1515/znb-1972-0213. [DOI] [PubMed] [Google Scholar]
  5. Saunders J. A., Conn E. E., Lin C. H., Shimada M. Localization of Cinnamic Acid 4-Monooxygenase and the Membrane-bound Enzyme System for Dhurrin Biosynthesis in Sorghum Seedlings. Plant Physiol. 1977 Oct;60(4):629–634. doi: 10.1104/pp.60.4.629. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Schaffner W., Weissmann C. A rapid, sensitive, and specific method for the determination of protein in dilute solution. Anal Biochem. 1973 Dec;56(2):502–514. doi: 10.1016/0003-2697(73)90217-0. [DOI] [PubMed] [Google Scholar]
  7. Thayer S. S., Conn E. E. Subcellular Localization of Dhurrin beta-Glucosidase and Hydroxynitrile Lyase in the Mesophyll Cells of Sorghum Leaf Blades. Plant Physiol. 1981 Apr;67(4):617–622. doi: 10.1104/pp.67.4.617. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Plant Physiology are provided here courtesy of Oxford University Press

RESOURCES