Horseradish peroxidase-catalyzed oligomerization of ferulic acid on a template of a tyrosine-containing tripeptide

被引:31
|
作者
Oudgenoeg, G
Dirksen, E
Ingemann, S
Hilhorst, R
Gruppen, H
Boeriu, CG
Piersma, SR
van Berkel, WJH
Laane, C
Voragen, AGJ
机构
[1] Ctr Prot Technol TNO WU, NL-6700 EV Wageningen, Netherlands
[2] Univ Wageningen & Res Ctr, Dept Agrotechnol & Food Sci, Biochem Lab, NL-6703 HA Wageningen, Netherlands
[3] Univ Wageningen & Res Ctr, Dept Agrotechnol & Food Sci, Food Chem Lab, NL-6700 EV Wageningen, Netherlands
[4] Univ Amsterdam, Fac Sci, Swammerdam Inst Life Sci, NL-1018 WV Amsterdam, Netherlands
[5] ATO, NL-6708 PD Wageningen, Netherlands
[6] TNO Food & Nutr Res, NL-3700 AJ Zeist, Netherlands
关键词
D O I
10.1074/jbc.M201679200
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Ferulic acid (FA) is an abundantly present phenolic constituent of plant cell walls. Kinetically controlled incubation of FA and the tripeptide Gly-Tyr-Gly (GYG) with horseradish peroxidase and H2O2 yielded a range of new cross-linked products. Two predominant series of hetero-oligomers of FA linked by dehydrogenation to the peptidyl tyrosine were characterized by electrospray ionization (tandem) mass spectrometry. One series comprises GYG coupled with 4-7 FA moieties linked by dehydrogenation, of which one is decarboxylated. In the second series 4-9 FA moieties linked by dehydrogenation, of which two are decarboxylated, are coupled to the tripeptide. A third series comprises three hetero-oligomers in which the peptidyl tyrosine is linked to 1-3 FA moieties of which none is decarboxylated. Two mechanisms for the formation of the FA-Tyr oligomers that result from the dualistic, concentration-dependent chemistry of FA and their possible role in the regulation of plant cell wall tissue growth are presented.
引用
收藏
页码:21332 / 21340
页数:9
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