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Purification and characterization of sinapine synthase from seeds of Brassica napus.

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.

journal_name

Arch Biochem Biophys

journal_title

Archives of biochemistry and biophysics

authors

Vogt T,Aebershold R,Ellis B

doi

10.1006/abbi.1993.1086

subject

Has Abstract

pub_date

1993-02-01 00:00:00

pages

622-8

issue

2

eissn

0003-9861

issn

1096-0384

pii

S0003-9861(83)71086-6

journal_volume

300

pub_type

杂志文章

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