大肠杆菌β-N-乙酰氨基葡萄糖苷酶的分子特征及其在细胞壁循环利用中的作用。
Molecular characterization of the beta-N-acetylglucosaminidase of Escherichia coli and its role in cell wall recycling.
作者信息
Cheng Q, Li H, Merdek K, Park J T
机构信息
Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, Massachusetts 02111, USA.
出版信息
J Bacteriol. 2000 Sep;182(17):4836-40. doi: 10.1128/JB.182.17.4836-4840.2000.
Abstract
The beta-N-acetylglucosaminidase of Escherichia coli was found to have a novel specificity and to be encoded by a gene (nagZ) that maps at 25.1 min. It corresponds to an open reading frame, ycfO, whose predicted amino acid sequence is 57% identical to that of Vibrio furnissii ExoII. NagZ hydrolyzes the beta-1,4 glycosidic bond between N-acetylglucosamine and anhydro-N-acetylmuramic acid in cell wall degradation products following their importation into the cell during the process for recycling cell wall muropeptides. From amino acid sequence comparisons, the novel beta-N-acetylglucosaminidase appears to be conserved in all 12 gram-negative bacteria whose complete or partial genome sequence data are available.
摘要
已发现大肠杆菌的β-N-乙酰氨基葡萄糖苷酶具有一种新的特异性，且由位于25.1分钟处的一个基因（nagZ）编码。它对应于一个开放阅读框ycfO，其预测的氨基酸序列与弗氏弧菌外切酶II的氨基酸序列有57%的同一性。在细胞壁肽聚糖循环利用过程中，细胞壁降解产物被导入细胞后，NagZ会水解N-乙酰氨基葡萄糖和脱水N-乙酰胞壁酸之间的β-1,4糖苷键。通过氨基酸序列比较，这种新的β-N-乙酰氨基葡萄糖苷酶似乎在所有12种已获得完整或部分基因组序列数据的革兰氏阴性细菌中都是保守的。
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