Complete amino acid sequence of alpha-acetolactate decarboxylase from Bacillus brevis.

I Svendsen, B R Jensen, M Ottesen
{"title":"Complete amino acid sequence of alpha-acetolactate decarboxylase from Bacillus brevis.","authors":"I Svendsen,&nbsp;B R Jensen,&nbsp;M Ottesen","doi":"10.1007/BF02907185","DOIUrl":null,"url":null,"abstract":"<p><p>The complete amino acid sequence of acetolactate decarboxylase (EC 4.1.1.5) from Bacillus brevis has been determined by sequencing of the intact enzyme and of peptides obtained by cleavage with cyanogen bromide, Staphylococcus aureus V8 protease and trypsin, respectively. Determination of the C-terminal part was made by treatment with carboxypeptidases Y and M II. The enzyme has a molecular weight of 29,093 and consists of 260 amino acid residues arranged in a single peptide chain without disulphide bonds.</p>","PeriodicalId":9616,"journal":{"name":"Carlsberg Research Communications","volume":"54 4","pages":"157-63"},"PeriodicalIF":0.0000,"publicationDate":"1989-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF02907185","citationCount":"5","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Carlsberg Research Communications","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1007/BF02907185","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 5

Abstract

The complete amino acid sequence of acetolactate decarboxylase (EC 4.1.1.5) from Bacillus brevis has been determined by sequencing of the intact enzyme and of peptides obtained by cleavage with cyanogen bromide, Staphylococcus aureus V8 protease and trypsin, respectively. Determination of the C-terminal part was made by treatment with carboxypeptidases Y and M II. The enzyme has a molecular weight of 29,093 and consists of 260 amino acid residues arranged in a single peptide chain without disulphide bonds.

短芽孢杆菌α -乙酰乳酸脱羧酶的完整氨基酸序列。
通过对短芽孢杆菌乙酰乳酸脱羧酶(EC 4.1.1.5)的完整酶和与溴化氰、金黄色葡萄球菌V8蛋白酶和胰蛋白酶裂解得到的肽的测序,确定了短芽孢杆菌乙酰乳酸脱羧酶的完整氨基酸序列。羧基肽酶Y和M II对c端进行了测定。该酶的分子量为29,093,由260个氨基酸残基排列在一条没有二硫键的单肽链上。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
自引率
0.00%
发文量
0
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信