Laccase-catalyzed carbon-nitrogen bond formation: coupling and derivatization of unprotected L-phenylalanine with different para-hydroquinones.
Unprotected L-phenylalanine was derivatized by an innovative enzymatic method by means of laccases from Pycnoporus cinnabarinus and Myceliophthora thermophila. During the incubation of L-phenylalanine with para-hydroquinones using laccase as biocatalyst, one or two main products were formed. Dependent on the substitution grade of the hydroquinones mono- and diaminated products were detected. Differences of the used laccases are discussed. The described reactions are of interest for the derivatization of amino acids and a synthesis of pharmacological-active amino acid structures in the field of white biotechnology.
Hahn
V
V
Institut für Mikrobiologie, Ernst-Moritz-Arndt-Universität Greifswald, F.-L.-Jahnstr. 15, 17487 Greifswald, Germany. veronikahahn@gmx.at
Mikolasch
A
A
Manda
K
K
Gördes
D
D
Thurow
K
K
Schauer
F
F
D002244:Carbon / Q000737:chemistry / Q000378:metabolism*; D005656:Fungal Proteins / Q000378:metabolism*; D006873:Hydroquinones / Q000737:chemistry / Q000378:metabolism; D042845:Laccase / Q000378:metabolism*; D015394:Molecular Structure; D009584:Nitrogen / Q000737:chemistry*; D010649:Phenylalanine / Q000737:chemistry / Q000378:metabolism; D055494:Pycnoporus / Q000201:enzymology
D005656:Fungal Proteins; D006873:Hydroquinones; D010649:Phenylalanine; D002244:Carbon; D042845:Laccase; D009584:Nitrogen