17263-44-4Relevant articles and documents
Enzymatic C-terminal amidation of amino acids and peptides
Nuijens, Timo,Piva, Elena,Kruijtzer, John A.W.,Rijkers, Dirk T.S.,Liskamp, Rob M.J.,Quaedflieg, Peter J.L.M.
experimental part, p. 3777 - 3779 (2012/09/22)
Herein, we describe two versatile and high yielding enzymatic approaches for the conversion of semi-protected amino acid and peptidyl C-terminal α-carboxylic acids into their corresponding amides. In the first approach, the lipase Candida antarctica lipase-B (Cal-B), and in the second approach, the protease Subtilisin A, are used, respectively. We found that by using the ammonium salt of the α-carboxylic acid instead of separate ammonia sources, the enzymatic amidation reactions proceeded much faster without side reactions and gave near to quantitative yields of products.
C-terminal peptide amidation catalyzed by orange flavedo peptide amidase
Cerovsky, Vaclav,Kula, Maria-Regina
, p. 1885 - 1887 (2007/10/03)
The reverse reaction of amide hydrolysis can be achieved with the peptide amidase derived from oranges [Eq(1); Z=benzyloxycarbonyl]. The C-terminal carboxy group of the peptide is directly converted into an amide group by condensation with an ammonium salt. The amidation of peptides is of major interest since the biological activity of proteohormones and peptides is strongly influenced by the presence of a C-terminal amide group.
