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Two flavonoid-specific malonyltransferases from cell suspension cultures ofPetroselinum hortense: Partial purification and some properties of malonyl-coenzyme A: Flavone/flavonol-7-O-glycoside malonyltransferase and malonyl-coenzyme A: Flavonol-3-O-glucoside malonyltransferase

Authors
Journal
Archives of Biochemistry and Biophysics
0003-9861
Publisher
Elsevier
Publication Date
Volume
208
Issue
1
Identifiers
DOI: 10.1016/0003-9861(81)90145-4
Keywords
  • Photosynthesis And Plant Biochemistry
Disciplines
  • Biology

Abstract

Abstract Two malonyltransferases were isolated from irradiated cell suspension cultures of parsley ( Petroselinum hortense) and extensively purified. One enzyme was most active with flavone and flavonol 7- O-glycosides as substrates; the other enzyme preferentially malonylated flavonol 3- O-glucosides. The substrate specificity of the enzymes in vitro was in good agreement with the pattern of malonylated flavonoid glycosides occurring in the cell cultures in vivo. The apparent K m values for the most efficient substrates, including the donor of the acyl residue, malonyl-CoA, were about 4–20 μ m. Both malonyltransferases had an apparent molecular weight of approximately 50,000.

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