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  • Title: Purification and characterization of sinapine synthase from seeds of Brassica napus.
    Author: Vogt T, Aebershold R, Ellis B.
    Journal: Arch Biochem Biophys; 1993 Feb 01; 300(2):622-8. PubMed ID: 8382030.
    Abstract:
    1-O-Sinapoylglucose:choline sinapoyltransferase ("sinapine synthase") has been purified from immature seeds of Brassica napus by sequential hydroxylapatite absorption, ion-exchange chromatography, and gel filtration. The purified enzyme has an apparent molecular weight of 65 kDa on gel filtration and a subunit structure on sodium dodecyl sulfate-polyacrylamide gel electrophoresis of 28 kDa. Sinapine synthase has Km values in the high micromolar range for both substrates (1-O-sinapoylglucose and choline chloride) but these values are sensitive to the concentration of the second substrate. The enzyme displays a marked substrate specificity for 1-O-sinapoylglucose among other related glucose esters. No requirements for thiol protectants or divalent cations were found, but sinapine synthase activity is inhibited by Cu2+ and Hg2+ ions. Partial amino acid sequence data have been obtained from a tryptic digest of the 28-kDa polypeptide.
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