Journal
AMINO ACIDS
Volume 31, Issue 4, Pages 409-419Publisher
SPRINGER WIEN
DOI: 10.1007/s00726-005-0276-8
Keywords
laccase; cross-coupling; derivatisation; tryptophan; unprotected amino acid; Pycnoporus cinnabarinus
Categories
Ask authors/readers for more resources
We have studied the enzymatic derivatization of amino acids by use of the polyphenol oxidase laccase. Derivatization of L-tryptophan was achieved by enzymatic crosslinking with the laccase substrate 2,5-dihydroxy-N-(2-hydroxyethyl)-benzamide. The main product (yield up to 70%) was identified as the quinoid compound 2-[2-(2-hydroxy-ethylcarbamoyl)-3,6-dioxo-cyclohexa-1,4-dienylamino]-3-(1H-indol-3-yl)- propionic acid and demonstrates that laccase-catalyzed C-N-coupling occurred on the amino group of the aliphatic side chain. These enzyme based reactions provide a simple and fast method for the derivatization of unprotected amino acids.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available