The C-terminal α-amide formation of the peptides is one of the most important events of prohormone processing. We have recently isolated an α-amidating enzyme, AE-I, from Xenopus laevis skin, which is the only enzyme ever purified to homogeneity. In this study, we report cloning and sequence of cDNA encoding AE-I. Our results indicate that enzyme AE-I is initially synthesized as a precursor with 400 amino acid residues, which is further processed to the mature enzyme consisting of 344 residues. Preliminary expression in E. coli of the cDNA corresponding to AE-I was found to produce an enzyme with appreciable α-amidating activity.
|Number of pages||7|
|Journal||Biochemical and biophysical research communications|
|Publication status||Published - 1987 Oct 29|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology