Invited Review D-Amino Acids in Animal Peptides

2008 
Summary. Secreted peptides from diverse sources have been found to contain a D-amino acid. From the sequence of cloned mRNAs coding for the precursors of such peptides it could be deduced that in all cases tested so far the D-amino acid in the final product is derived from the corresponding L-amino acid present in the primary product of translation. Enzymes catalyzing such an L -t oD-isomerization in peptide linkage have been isolated from the venom of a spider and the skin secretions of frogs. Even though these are completely different proteins, the reaction mechanism is the same, namely a deprotonation=re-protonation of the � -carbon of an amino acid with concomitant inversion of the chirality. Sequences potentially coding for homologues of the frog enzyme are present in the genome of different vertebrate species.
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