Enzymatic synthesis of dipeptide units of the D-D-configuration in aqueous media

Maria Kempe, Björn Ekberg, Klaus Mosbach

Research output: Contribution to journalArticlepeer-review


The enzymatic synthesis of dipeptide units of the d-d-configuration in aqueous media, catalysed by muramoyl-pentapeptide carboxypeptidase (E.C., is described. Ac-l-Lys(Ac)-d-Ala-d-Lac-OH and Ac-d-Ala-OMe were used as acyl-components. Neutral, basic, and hydrophobic amino acids acting as nucleophiles were incorporated. The enzyme is stereospecific in that only the d-enantiomers of amino acids or amino acid derivatives were incorporated. As nucleophiles, the unmodified amino acids resulted in higher product yields compared with using the corresponding amino acid derivatives. Product yields ranged from 40 to 87%
Original languageEnglish
Pages (from-to)147-152
JournalInternational Journal of Peptide and Protein Research
Issue number2
Publication statusPublished - 1990

Subject classification (UKÄ)

  • Biochemistry and Molecular Biology


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