Titre du document / Document title
Purification and characterization of anthocyanin 3-aromatic acyltransferase from Perilla frutescens
Auteur(s) / Author(s)
FUJIWARA H. (1) ;
TANAKA Y. (1) ;
FUKUI Y. (1) ;
ASHIKARI T. (1) ;
YAMAGUCHI M. (2) ;
KUSUMI T. (1) ;
Affiliation(s) du ou des auteurs / Author(s) Affiliation(s)
(1) Institute for Fundamental Research, Suntory Ltd., 1-1-1, Wakayamadai, Shimamoto-cho, Mishima-gun, Osaka 618-8503, JAPON
(2) Department of Food Science and Technology, Minami-Kyushu University, Takanabe, Miyazaki 884-0000, JAPON
Résumé / Abstract
Hydroxycinnamoyl-CoA:anthocyanin 3-O-glucoside-6-O-hydroxycinnamoyltransferase (3AT: EC 2.3.1.-) was identified and highly purified from red leaves of Perilla frutescens, which accumulate cyanidin 3-(6-O-p-coumaroyl-β- D-glucoside)-5-(6-O-malonyl-β-D-glucoside). 3AT was a 50 kDa monomer of protein with a pI of 5.3. It catalyzed the transfer of the p-coumaric and caffeic acids from their CoA esters to the 3-glucosyl moiety of delphinidin, cyanidin and pelargonidin 3-glucoside. Anthocyanidin 3.5-diglucosides were also good substrates. while cyanidin 3-rutinoside was a poor substrate. Malonyl-CoA was not used by the enzyme as an acyl-donor. Aromatic acylation of anthocyanin by 3AT caused a bathochromic shift. Lower K, values for anthocyanidin 3-glucoside than 3,5-diglucoside may indicate that acylation of cyanidin 3-glucoside precedes 5-O-glucosylation in vivo.
Revue / Journal Title
Plant science
ISSN
0168-9452
CODEN PLSCE4
Source / Source
1998, vol. 137, n
o1, pp. 87-94 (19 ref.)
Langue / Language
Anglais
Editeur / Publisher
Elsevier, Shannon, IRLANDE
(1985)
(Revue)
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Localisation / Location
INIST-CNRS, Cote INIST : 15982, 35400007108484.0080
Nº notice refdoc (ud4) : 2414423
