期刊
ANALYTICAL BIOCHEMISTRY
卷 302, 期 1, 页码 70-74出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1006/abio.2001.5522
关键词
ascidian; 3,4-dihydroxyphenylalanine; mussel; posttranslational modification; 3,4,5-trihydroxyphenylalanine; tyrosinase
An improved method for hydroxylating tyrosine-containing sequences in polypeptides to peptidyl 3,4-dihydroxyphenylalanine (DOPA) using mushroom tyrosinase at relatively high enzyme-to-substrate ratios is described. The new method involves incorporating borate into the reaction mixture to stop formation of the unwanted side product 3,4,5-trihydroxyphenylalanine. Using this method, a model for the palindromic central sequence for the antimicrobial peptide family, the styelins, Y*Y*KHKY*Y* (where Y* is DOPA), was successfully synthesized in high yield from YYKHKYY. This sequence represents a particularly challenging target because of the cluster of four precursor tyrosine residues are in close proximity. The method should be readily applied to larger polypeptides produced by either solid-phase synthesis or recombinant techniques and give greater insight into the roles of this unusual posttranslational modification in marine invertebrates such as mussels and ascidians. (C) 2002 Elsevier Science (USA).
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