Monatshefte für Chemie - Chemical Monthly

, Volume 139, Issue 1, pp 1–5

d-Amino Acids in Animal Peptides

Invited Review

DOI: 10.1007/s00706-007-0780-5

Cite this article as:
Jilek, A. & Kreil, G. Monatsh. Chem. (2008) 139: 1. doi:10.1007/s00706-007-0780-5

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- to d-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 de-protonation/re-protonation of the α-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.

Keywords. Peptides; Enantiomerization; Isomerase; Chiral inversion. 

Copyright information

© Springer-Verlag 2007

Authors and Affiliations

  1. 1.Institute of Organic ChemistryJohannes Kepler University LinzLinzAustria
  2. 2.Institute of Physiology and PathophysiologyParacelsus Medical UniversitySalzburgAustria

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