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首页> 外文期刊>The Journal of Antibiotics: An International Journal >Molecular Cloning and Sequencing of the Edeine B_1 Amidinohydrolase Gene of Bacillus brevis TT02-8 and Its Expression in Escherichia coli
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Molecular Cloning and Sequencing of the Edeine B_1 Amidinohydrolase Gene of Bacillus brevis TT02-8 and Its Expression in Escherichia coli

机译：短芽孢杆菌TT02-8 Edeine B_1酰胺水解酶基因的分子克隆，序列分析及其在大肠杆菌中的表达

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摘要

The gene encoding edeine B_1 amidinohydrolase from Bacillus brevis TT02-8 was cloned into Escherichia coli and its nucleotide sequence was determined.An open reading frame was identified and ws found to encode a polypeptide of 289 amino acid residues with a predicted molecular weight of 32,455,which was consistent with that previously calculated for edeine B_1 amidinohydrolase purified from this bacterium.Comparison of the deduced amino acid sequence of this enzyme with other amidinohydrolases revealed the highest homology to B. subtilis agmatine ureohydolase.The enzymatic activity of the protein produced in Escherichia coli was analyzed .Three histidine residues.H-112,H-137 and H-151 in the edeine B_1 amidinohydrolase,which are highly conserved in amidinohydrolases,were changed to alanine by site-directed mutagenesis.Analysis of each of these mutants revealed that three histidine residues are important but not essential for the enzyme activity.
机译：将来自短芽孢杆菌TT02-8的乙二胺乙水解酶基因克隆到大肠杆菌中，确定其核苷酸序列，确定一个开放阅读框，发现其编码289个氨基酸残基的多肽，预测分子量为32,455，该酶的推导氨基酸序列与其他酰胺水解酶的氨基酸序列比较显示，与枯草芽孢杆菌胍丁胺脲醛缩酶的同源性最高。乙胺水解酶中高度保守的乙二胺B_1酰胺水解酶中的三个组氨酸残基H-112，H-137和H-151通过定点诱变变为丙氨酸。每个突变体的分析表明，三个组氨酸残基对酶活性很重要但不是必需的。

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