Document Detail


Laccase-catalyzed carbon-nitrogen bond formation: coupling and derivatization of unprotected L-phenylalanine with different para-hydroquinones.
MedLine Citation:
PMID:  18695937     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
V Hahn; A Mikolasch; K Manda; D G??rdes; K Thurow; F Schauer
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2008-08-10
Journal Detail:
Title:  Amino acids     Volume:  37     ISSN:  1438-2199     ISO Abbreviation:  Amino Acids     Publication Date:  2009 Jul 
Date Detail:
Created Date:  2009-07-06     Completed Date:  2009-12-23     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9200312     Medline TA:  Amino Acids     Country:  Austria    
Other Details:
Languages:  eng     Pagination:  315-21     Citation Subset:  IM    
Affiliation:
Institut f??r Mikrobiologie, Ernst-Moritz-Arndt-Universit??t Greifswald, F.-L.-Jahnstr. 15, 17487 Greifswald, Germany. veronikahahn@gmx.at
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MeSH Terms
Descriptor/Qualifier:
Carbon / chemistry,  metabolism*
Fungal Proteins / metabolism*
Hydroquinones* / chemistry,  metabolism
Laccase / metabolism*
Molecular Structure
Nitrogen / chemistry*
Phenylalanine* / chemistry,  metabolism
Pycnoporus / enzymology
Chemical
Reg. No./Substance:
0/Fungal Proteins; 0/Hydroquinones; 63-91-2/Phenylalanine; 7440-44-0/Carbon; 7727-37-9/Nitrogen; EC 1.10.3.2/Laccase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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