Properties and genetic control of four methyltransferases involved in methylation of anthocyanins in flowers of Petunia hybrida
- 1 February 1984
- journal article
- research article
- Published by Springer Nature in Planta
- Vol. 160 (2) , 174-179
- https://doi.org/10.1007/bf00392867
Abstract
Four S-adenosyl-l-methionine:anthocyanin-3′,5′-O-methyltransferases in flowers of Petunia hybrida were separated using the chromatofocusing technique. Each methyltransferase is controlled by one of the methylation genes Mt1, Mt2, Mf1 or Mf2. Molecular weight, pH-activity optimum, isoelectric point, several kinetic properties and the behaviour in the presence of Mg2+, ethylenediaminetetraacetic acid and S-adenosyl-l-homocysteine of each of the four enzymes were determined. The methylation in vitro of delphinidin 3-(p-coumaroyl)-rutinosido-5-glucoside reflected the accumulation patterns of methylated anthocyanins in vivo and established the regulatory role of methyltransferases in vivo.Keywords
This publication has 15 references indexed in Scilit:
- Genetic control of anthocyanin-O-methyltransferase activity in flowers of Petunia hybridaTheoretical and Applied Genetics, 1983
- Characterization of three distinct flavonol O-methyltransferases from Chrysosplenium americanumPhytochemistry, 1982
- Methylation of anthocyanins by cell-free extracts of flower buds of Petunia hybridaPhytochemistry, 1982
- Genetic control of chalcone isomerase activity in anthers of Petunia hybridaPlanta, 1979
- O-methylation of flavonoid substrates by a partially purified enzyme from soybean cell suspension culturesArchives of Biochemistry and Biophysics, 1977
- A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye BindingAnalytical Biochemistry, 1976
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Purification and properties of : Caffeic acid o-methyltransferase from leaves of spinach Beet (Beta vulgaris L.)Biochimica et Biophysica Acta (BBA) - Enzymology, 1975
- Purification and Properties of a S‐Adenosylmethionine: Isoflavone 4′‐O‐Methyltransferase from Cell Suspension Cultures of Cicer arietinum L.European Journal of Biochemistry, 1974
- Purification and properties of an o-dihydricphenol meta-O-methyltransferase from cell suspension cultures of parsley and its relation to flavonoid biosynthesisBiochimica et Biophysica Acta (BBA) - Enzymology, 1972