TY - JOUR
T1 - Cloning and sequence of cDNA encoding a peptide C-terminal α-amidating enzyme from Xenopus laevis
AU - Mizuno, Kensaku
AU - Ohsuye, Kazuhiro
AU - Wada, Yayoi
AU - Fuchimura, Kayoko
AU - Tanaka, Shoji
AU - Matsuo, Hisayuki
PY - 1987/10/29
Y1 - 1987/10/29
N2 - 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.
AB - 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.
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U2 - 10.1016/0006-291X(87)90911-9
DO - 10.1016/0006-291X(87)90911-9
M3 - Article
C2 - 3689360
AN - SCOPUS:0023667622
VL - 148
SP - 546
EP - 552
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 2
ER -