THE NEGATIVE REGULATOR OF BETA-LACTAMASE INDUCTION AMPD IS A N-ACETYL-ANHYDROMURAMYL-L-ALANINE AMIDASE
THE NEGATIVE REGULATOR OF BETA-LACTAMASE INDUCTION AMPD IS A N-ACETYL-ANHYDROMURAMYL-L-ALANINE AMIDASE
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DOI：
10.1111/j.1574-6968.1994.tb07159.x
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发表时间：
1994-09-15
影响因子：
2.1
通讯作者：
WIEDEMANN, B
中科院分区：
文献类型：
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作者：
HOLTJE, JV;KOPP, U;WIEDEMANN, B
malE-ampD基因融合体的构建允许通过亲和层析纯化具有生物活性的融合蛋白。克隆的malE-ampD基因融合体补充了染色体ampD突变。纯化的MalE-AmpD融合蛋白被发现具有胞壁素酰胺酶活性，对大肠杆菌中的特征胞壁素周转产物1，6-脱水胞壁肽具有显著的特异性。AmpD是一种N-乙酰-脱水胞壁酰-L-丙氨酸酰胺酶，可能参与周转产物的再循环。这表明AmpD的负调节作用是由于水解脱水-胞肽，这可能是β-内酰胺酶诱导的信号。
Construction of a malE-ampD gene fusion allowed purification of biologically active fusion protein by affinity chromatography. The cloned malE-ampD gene fusion complemented a chromosomal ampD mutation. Purified MalE-AmpD fusion protein was found to have murein amidase activity with a pronounced specificity for 1,6-anhydromuropeptides, the characteristic murein turnover products in Escherichia coli. Being a N-acetyl-anhydromuramyl-L-alanine amidase AmpD is likely to be involved in recycling of the turnover products. It is suggested that the negative regulatory effect of AmpD is due to the hydrolysis of anhydro-muropeptides which may function as signals for beta-lactamase induction.