Laccase-induced derivatization of unprotected amino acid L-tryptophan by coupling with p-hydroquinone 2,5-dihydroxy-N-(2-hydroxyethyl)-benzamide.
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.
Institut für Mikrobiologie, Ernst-Moritz-Arndt-Universität Greifswald, Greifswald, Germany.
K
K
Manda
E
E
Hammer
A
A
Mikolasch
D
D
Gördes
K
K
Thurow
F
F
Schauer
D001549:Benzamides / Q000737:chemistry*; D006873:Hydroquinones / Q000737:chemistry* / Q000378:metabolism; D042845:Laccase / Q000302:isolation & purification / Q000378:metabolism*; D014364:Tryptophan / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism
D001549:Benzamides; D006873:Hydroquinones; D014364:Tryptophan; D042845:Laccase; C526576:2,5-dihydroxy-N-(2-hydroxyethyl)benzamide; C031927:hydroquinone