Two enzymes concerned in peptide hormone alpha-amidation are synthesized from a single mRNA.
By expressing truncated rat pituitary 'peptidylglycine alpha-amidating enzyme' cDNAs in COS-7 cells, we found that the two reactions concerned in peptide carboxyl-terminal amidation, namely the peptidylglycine alpha-hydroxylation reaction and the peptidyl-hydroxyglycine amidation reaction, were catalyzed by 37- and 53-K proteins, which were derived from the 5'- and 3'-coding sequences, respectively. The full-length cDNA directed the expression of both the 37- and 53-K enzymes, and in the combined presence of the two enzymes the full conversion of a glycine-extended peptide into the amidated product was achieved. These results indicated that two enzymes concerned in peptide hormone alpha-amidation are generated from a common precursor protein encoded by a single mRNA.
Department of Biochemistry, Tohoku University School of Medicine, Miyagi, Japan.
I
I
Kato
H
H
Yonekura
M
M
Tajima
M
M
Yanagi
H
H
Yamamoto
H
H
Okamoto
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D015152:Blotting, Northern; D002460:Cell Line; D002850:Chromatography, Gel; D006899:Mixed Function Oxygenases / Q000096:biosynthesis / Q000235:genetics* / Q000302:isolation & purification; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009097:Multienzyme Complexes; D015345:Oligonucleotide Probes; D009842:Oligopeptides / Q000138:chemical synthesis; D010902:Pituitary Gland / Q000201:enzymology*; D010957:Plasmids; D012313:RNA / Q000235:genetics / Q000302:isolation & purification; D012326:RNA Splicing; D012333:RNA, Messenger / Q000235:genetics*; D051381:Rats; D013379:Substrate Specificity; D014162:Transfection
D009097:Multienzyme Complexes; D015345:Oligonucleotide Probes; D009842:Oligopeptides; D012333:RNA, Messenger; D012313:RNA; D006899:Mixed Function Oxygenases; C035189:peptidylglycine monooxygenase