| Literature DB >> 6497385 |
J Koester, R Bussmann, W Barz.
Abstract
A malonyltransferase which catalyzes the malonylation of isoflavone 7-O-glucosides in position 6 of the glucose moiety using malonyl-coenzyme A as acyl donor has been purified 157-fold from 4-day-old roots of chick pea (Cicer arietinum L.). The enzyme showed a pH optimum of 8.0 and a molecular weight of 112,000. The Km for malonylcoenzyme A was 48 microM and, for the chick pea isoflavones biochanin A and formononetin, 36 and 24 microM, respectively. Various other isoflavone, flavone, and flavonol 7-O-glucosides and chalcone 4'-O-glucosides were much poorer substrates. Flavonol 3-O-glucosides and isoflavone 4'-O-glucosides were not malonylated by the malonyltransferase.Entities:
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Year: 1984 PMID: 6497385 DOI: 10.1016/0003-9861(84)90298-4
Source DB: PubMed Journal: Arch Biochem Biophys ISSN: 0003-9861 Impact factor: 4.013