大肠杆菌
生物
基因
拉伤
重组DNA
聚合酶链反应
酶
系统发育树
遗传学
分子生物学
生物化学
解剖
作者
David Saul,Liam Williams,Helen S. Toogood,Roy M. Daniel,Peter L. Bergquist
出处
期刊:Biochimica et biophysica acta (N)
[Elsevier]
日期:1996-07-01
卷期号:1308 (1): 74-80
被引量:18
标识
DOI:10.1016/0167-4781(96)00074-7
摘要
The gene for a highly thermostable neutral proteinase (Npr) was isolated from Bacillus sp. strain EA1 by the polymerase chain reaction using consensus primers based on the sequences of npr genes from related species. The gene was sequenced and shown to be closely related to a neutral proteinase gene from Bacillus caldolyticus strain YP-T; the mature form of the enzyme differing by only a single amino acid. Enzyme samples were prepared from both the native organisms and also from recombinant Escherichia coli expressing the two npr genes. The proteinase from strain EA1 was shown to be significantly more thermostable than that from B. caldolyticus and that this difference is the result of a single amino acid substitution which is situated proximal to a region of the enzyme known to be crucial to conferring thermal stability. The phylogenetic relationship of EA1 to other Bacilli is also described.
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