Enzymatic synthesis of dipeptide units of the D-D-configuration in aqueous media.
The enzymatic synthesis of dipeptide units of the D-D-configuration in aqueous media, catalysed by muramoyl-pentapeptide carboxypeptidase (E.C.3.4.17.8), 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%.
Department of Pure and Applied Biochemistry, University of Lund, Sweden.
M
M
Kempe
B
B
Ekberg
K
K
Mosbach
D000595:Amino Acid Sequence; D002511:Cephalosporins; D055598:Chemical Phenomena; D002621:Chemistry; D004151:Dipeptides; D006868:Hydrolysis; D008969:Molecular Sequence Data; D002267:Muramoylpentapeptide Carboxypeptidase; D010400:Penicillin G; D012997:Solvents; D013237:Stereoisomerism
D002511:Cephalosporins; D004151:Dipeptides; D012997:Solvents; D002267:Muramoylpentapeptide Carboxypeptidase; D010400:Penicillin G