Molecular characterization of the β-N-acetylglucosaminidase of Escherichia coli and its role in cell wall recycling
Molecular characterization of the β-N-acetylglucosaminidase of Escherichia coli and its role in cell wall recycling
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DOI：
10.1128/jb.182.17.4836-4840.2000
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发表时间：
2000-09-01
影响因子：
3.2
通讯作者：
Park, JT
中科院分区：
文献类型：
--
作者：
Cheng, QM;Li, HS;Park, JT
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，其编码基因(NagZ)的映射时间为25.1分钟。它对应于一个开放阅读框ycfO，其预测的氨基酸序列与华氏弧菌ExoII的氨基酸序列有57%的同源性。在回收细胞壁多肽的过程中，NagZ将细胞壁降解产物中的N-乙酰氨基葡萄糖和脱水-N-乙酰胞壁酸之间的β-1，4糖苷键输入细胞，使其发生水解性反应。从氨基酸序列比较，新的β-N-乙酰氨基葡萄糖苷酶似乎在所有12个革兰氏阴性菌中保守，其完整或部分基因组序列数据可用。
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.