Primary structure of carboxypeptidase III from malted barley.

S B Sørensen, I Svendsen, K Breddam
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引用次数: 43

Abstract

The primary structure of malt carboxypeptidase III has been determined. The enzyme is a single N-terminally blocked polypeptide chain containing 411 amino acid residues. The sequence of these amino acid residues was deduced from analysis of fragments of the polypeptide chain obtained by chemical cleavages with either cyanogen bromide or hydroxylamine and by enzymatic cleavages with either trypsin, S. aureus V8 protease or proteinase A from yeast. A glycosylated asparagine was found in position 71. The determined sequence was 97% homologous with the amino acid sequence derived from the nucleotide sequence of a gene coding for a wheat protein postulated to be a carboxypeptidase. The malt carboxypeptidase III sequence showed 34% homology with the amino acid sequence of the single-chain carboxypeptidase Y, and about 25% homology with the combined A- and B-chains of malt carboxypeptidase I and II as well as wheat carboxypeptidase II.

麦芽羧肽酶III的一级结构。
确定了麦芽羧肽酶III的一级结构。该酶是一个单一的n端阻断多肽链,含有411个氨基酸残基。这些氨基酸残基的序列是通过对多肽链片段的分析推断出来的,这些片段是通过与溴化氰或羟胺的化学裂解获得的,以及通过与胰蛋白酶、金黄色葡萄球菌V8蛋白酶或酵母蛋白酶A的酶切获得的。在第71位发现了糖基化的天冬酰胺。测定的序列与推定为羧肽酶的小麦蛋白基因编码的核苷酸序列同源性为97%。麦芽羧肽酶III序列与单链羧肽酶Y的氨基酸序列同源性为34%,与麦芽羧肽酶I和II的组合A链和b链以及小麦羧肽酶II的氨基酸序列同源性约为25%。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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