Horseradish peroxidase-catalyzed oligomerization of ferulic acid on a template of a tyrosine-containing tripeptide
article
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 heterooligomers 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. Chemicals/CAS: Coumaric Acids; ferulic acid, 1135-24-6; Glycine, 56-40-6; Horseradish Peroxidase, EC 1.11.1.-; Hydrogen Peroxide, 7722-84-1; Oxygen, 7782-44-7; Peptides; Tyrosine, 55520-40-6
Topics
TNO Identifier
87773
ISSN
00219258
Source
Journal of Biological Chemistry, 277(24), pp. 21332-21340.
Pages
21332-21340