In vitro biosynthesis of ring-extended cyclosporins.
Biochem J
; 300 ( Pt 2): 395-9, 1994 Jun 01.
Article
em En
| MEDLINE
| ID: mdl-8002944
ABSTRACT
Cyclosporin synthetase, a multifunctional polypeptide, catalyses the biosynthesis of the set of natural cyclosporins. We report that this enzyme is also capable of introducing a beta-alanine into position 7 or 8 of the ring instead of the alpha-alanines present at these positions in cyclosporin A. This leads to 34-membered rings in contrast to the 33-membered ring of the cyclo-undecapeptide cyclosporin A. Both [beta Ala7]CyA and [beta Ala8]CyA show immunosuppressive activity. The cyclosporin synthetase-related enzyme peptolide SDZ 214-103 synthetase, on the other hand, does not incorporate either beta-alanine into position 7 or beta-hydroxy acids into position 8, confirming the previously described higher substrate specificity of this enzyme compared with cyclosporin synthetase [Lawen and Traber (1993) J. Biol. Chem. 268, 20452-20465].
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Ciclosporinas
/
Fungos Mitospóricos
Idioma:
En
Revista:
Biochem J
Ano de publicação:
1994
Tipo de documento:
Article
País de afiliação:
Alemanha