Abstract:
:The C-terminal alpha-amide formation of the peptides is one of the most important events of prohormone processing. We have recently isolated an alpha-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 alpha-amidating activity.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Mizuno K,Ohsuye K,Wada Y,Fuchimura K,Tanaka S,Matsuo Hdoi
10.1016/0006-291x(87)90911-9subject
Has Abstractpub_date
1987-10-29 00:00:00pages
546-52issue
2eissn
0006-291Xissn
1090-2104pii
0006-291X(87)90911-9journal_volume
148pub_type
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