来自乳酸乳球菌乳脂亚种AM2的半胱氨酸氨肽酶基因pepC的克隆与测序
Cloning and sequencing of pepC, a cysteine aminopeptidase gene from Lactococcus lactis subsp. cremoris AM2.
作者信息
Chapot-Chartier M P, Nardi M, Chopin M C, Chopin A, Gripon J C
机构信息
Station de Recherches Laitières, Institut National de la Recherche Agronomique, Jouy-en-Josas, France.
出版信息
Appl Environ Microbiol. 1993 Jan;59(1):330-3. doi: 10.1128/aem.59.1.330-333.1993.
A gene coding for an aminopeptidase (PepC) from Lactococcus lactis subsp. cremoris AM2 was cloned by complementation of an Escherichia coli mutant lacking aminopeptidase activity. The nucleotide sequence was determined. A portion of the predicted amino acid sequence of PepC (436 amino acids) showed strong homology to the active site of cysteine proteases. No signal sequence was found, indicating an intracellular location of the enzyme.
通过对缺乏氨肽酶活性的大肠杆菌突变体进行互补，克隆了乳酸乳球菌乳脂亚种AM2中编码氨肽酶（PepC）的基因。测定了核苷酸序列。PepC预测氨基酸序列的一部分（436个氨基酸）与半胱氨酸蛋白酶的活性位点具有高度同源性。未发现信号序列，表明该酶定位于细胞内。
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