非洲爪蟾皮肤肽基羟甘氨酸N-C裂解酶的纯化及cDNA克隆，该酶催化C末端α-酰胺化的第二步反应。

Purification and cDNA cloning of Xenopus laevis skin peptidylhydroxyglycine N-C lyase, catalyzing the second reaction of C-terminal alpha-amidation.

作者信息

Iwasaki Y, Kawahara T, Shimoi H, Suzuki K, Ghisalba O, Kangawa K, Matsuo H, Nishikawa Y

机构信息

Bio-organics Research Department, International Research Laboratories, Ciba-Geigy, Japan.

出版信息

Eur J Biochem. 1991 Nov 1;201(3):551-9. doi: 10.1111/j.1432-1033.1991.tb16314.x.

DOI:10.1111/j.1432-1033.1991.tb16314.x

PMID:1935950

Abstract

The alpha-amidation of glycine-extended peptides is a two-step reaction catalyzed by peptidylglycine alpha-hydroxylating monooxygenase (PHM) and peptidylhydroxyglycine N-C lyase (PHL). PHL was purified to homogeneity from Xenopus laevis skin and its partial amino acid sequence (including the N-terminal 35 residues) was determined. It was found that the cDNA codes for a 935-residue precursor protein (AE-III protein), containing the PHM and PHL sequences at its N terminus and C terminus, respectively. The PHM sequence in AE-III protein is completely identical to that deduced from the nucleotide sequence of X. laevis AE-I cDNA, which encodes only PHM, except that the AE-I protein has an extra 10 residues at its C terminus. It is suggested that AE-I and AE-III mRNA are encoded by the same gene and produced by alternative splicing.

摘要

甘氨酸延伸肽的α-酰胺化是一个由肽基甘氨酸α-羟化单加氧酶（PHM）和肽基羟甘氨酸N-C裂解酶（PHL）催化的两步反应。从非洲爪蟾皮肤中纯化得到了均一的PHL，并测定了其部分氨基酸序列（包括N端的35个残基）。发现该cDNA编码一个935个残基的前体蛋白（AE-III蛋白），其N端和C端分别包含PHM和PHL序列。AE-III蛋白中的PHM序列与从非洲爪蟾AE-I cDNA的核苷酸序列推导出来的序列完全相同，AE-I cDNA仅编码PHM，只是AE-I蛋白在其C端有额外的10个残基。提示AE-I和AE-III mRNA由同一基因编码，并通过可变剪接产生。