Cloning and sequence of cDNA encoding a peptide C-terminal alpha-amidating enzyme from Xenopus laevis.

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.

authors

Mizuno K,Ohsuye K,Wada Y,Fuchimura K,Tanaka S,Matsuo H

doi

10.1016/0006-291x(87)90911-9

subject

Has Abstract

pub_date

1987-10-29 00:00:00

pages

546-52

issue

2

eissn

0006-291X

issn

1090-2104

pii

0006-291X(87)90911-9

journal_volume

148

pub_type

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