Cloning and sequence of cDNA encoding a peptide C-terminal alpha-amidating enzyme from Xenopus laevis.
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.
Mizuno
K
K
Department of Biochemistry, Miyazaki Medical College, Japan.
Ohsuye
K
K
Wada
Y
Y
Fuchimura
K
K
Tanaka
S
S
Matsuo
H
H
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D004247:DNA / Q000302:isolation & purification*; D006899:Mixed Function Oxygenases; D008969:Molecular Sequence Data; D009097:Multienzyme Complexes; D010105:Oxygenases / Q000235:genetics*; D012867:Skin / Q000201:enzymology; D014982:Xenopus laevis
D009097:Multienzyme Complexes; D004247:DNA; D006899:Mixed Function Oxygenases; D010105:Oxygenases; C035189:peptidylglycine monooxygenase