Enzymatic synthesis of dipeptide units of the D-D-configuration in aqueous media
(1990) In International Journal of Peptide and Protein Research 35(2). p.147-152- Abstract
- 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%
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1516048
- author
- Kempe, Maria LU ; Ekberg, Björn and Mosbach, Klaus LU
- organization
- publishing date
- 1990
- type
- Contribution to journal
- publication status
- published
- subject
- in
- International Journal of Peptide and Protein Research
- volume
- 35
- issue
- 2
- pages
- 147 - 152
- publisher
- Munksgaard Forlag
- external identifiers
-
- scopus:0025209791
- ISSN
- 0367-8377
- DOI
- 10.1111/j.1399-3011.1990.tb00250.x
- language
- English
- LU publication?
- yes
- id
- e749979e-d033-467f-92cc-5ffa37e65ad9 (old id 1516048)
- date added to LUP
- 2016-04-01 16:57:28
- date last changed
- 2021-01-03 10:53:37
@article{e749979e-d033-467f-92cc-5ffa37e65ad9, abstract = {{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%}}, author = {{Kempe, Maria and Ekberg, Björn and Mosbach, Klaus}}, issn = {{0367-8377}}, language = {{eng}}, number = {{2}}, pages = {{147--152}}, publisher = {{Munksgaard Forlag}}, series = {{International Journal of Peptide and Protein Research}}, title = {{Enzymatic synthesis of dipeptide units of the D-D-configuration in aqueous media}}, url = {{http://dx.doi.org/10.1111/j.1399-3011.1990.tb00250.x}}, doi = {{10.1111/j.1399-3011.1990.tb00250.x}}, volume = {{35}}, year = {{1990}}, }