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

I Svendsen, B R Jensen, M Ottesen
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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.

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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。
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