Cloning and primary structure of the wide-spectrum amidase from Brevibacterium sp. R312: high homology to the amiE product from Pseudomonas aeruginosa.
Cloning and primary structure of the wide-spectrum amidase from Brevibacterium sp. R312: high homology to the amiE product from Pseudomonas aeruginosa.
复制标题
短杆菌属广谱酰胺酶的克隆和一级结构。
DOI：
10.1016/0378-1119(92)90635-3
复制
发表时间：
1993
期刊：
影响因子：
3.5
通讯作者：
J. Crouzet
中科院分区：
文献类型：
--
作者：
F. Soubrier;S. Lévy;J. Mayaux;D. Pétré;A. Arnaud;J. Crouzet
ABrevibacteriumsp。利用纯化酶获得的有限氨基酸（aa）序列信息，对编码广谱酰胺酶（EC 3.5.1.4）的R312 DNA片段进行了克隆和测序。推导出的aa序列与该基因的产物铜绿假单胞菌脂肪酰胺酶有80%以上的严格一致性，表明该基因在革兰氏+菌和革兰氏−菌之间的进化过程中发生了水平转移。
ABrevibacteriumsp. R312 DNA fragment encoding the wide-spectrum amidase (EC 3.5.1.4) has been cloned and sequenced, using limited amino acid (aa) sequence information obtained from the purified enzyme. The deduced aa sequence showed more than 80% strict identity with thePseudomonas aeruginosaaliphatic amidase, the product of theamiEgene, suggesting a horizontal transfer of the gene during evolution between Gram+and Gram−bacteria.