Enzymic conversion of deuterated analogues of δ--α-aminoadipoyl--cysteinyl--allylglycine, an unnatural substrate for isopenicilin n synthase: A unified theory of second ring closure
التفاصيل البيبلوغرافية
العنوان:
Enzymic conversion of deuterated analogues of δ--α-aminoadipoyl--cysteinyl--allylglycine, an unnatural substrate for isopenicilin n synthase: A unified theory of second ring closure
The enzyme Isopenicillin N Synthase catalyses the conversion of the modified substrate δ- L -α-aminoadipoyl- L -cysteinyl- D -all to six β-lactam containing metabotites. Eight tripeptides deuterated in the allylglycine moiety have been prepared and the stereochemical course of their cyclization to the β-lactam containing metabolites has been investigated.
