Kato I, Yonekura H, Tajima M, Yanagi M, Yamamoto H, Okamoto H
Department of Biochemistry, Tohoku University School of Medicine, Miyagi, Japan.
Biochem Biophys Res Commun. 1990 Oct 15;172(1):197-203. doi: 10.1016/s0006-291x(05)80193-7.
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.
通过在COS-7细胞中表达截短的大鼠垂体“肽基甘氨酸α-酰胺化酶”cDNA，我们发现肽羧基末端酰胺化涉及的两个反应，即肽基甘氨酸α-羟基化反应和肽基羟基甘氨酸酰胺化反应，分别由源自5'-和3'-编码序列的37-K和53-K蛋白催化。全长cDNA指导了37-K和53-K两种酶的表达，并且在两种酶共同存在的情况下，实现了甘氨酸延伸肽向酰胺化产物的完全转化。这些结果表明，参与肽激素α-酰胺化的两种酶是由单个mRNA编码的共同前体蛋白产生的。
