THE LYTIC ENZYME OF THE PSEUDOMONAS PHAGE PHI-6 - PURIFICATION AND BIOCHEMICAL-CHARACTERIZATION
THE LYTIC ENZYME OF THE PSEUDOMONAS PHAGE PHI-6 - PURIFICATION AND BIOCHEMICAL-CHARACTERIZATION
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DOI：
10.1016/0167-4838(92)90073-m
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发表时间：
1992-09-04
期刊：
影响因子：
--
通讯作者：
BAMFORD, DH
中科院分区：
文献类型：
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作者：
CALDENTEY, J;BAMFORD, DH
含有脂质的噬菌体phi 6的裂解酶，蛋白质P5，已经从破碎的病毒颗粒中纯化至表观均一性。该酶是一种单体，分子量约为。24 kDa。P5活性的最适pH为8.5，该蛋白在20 ℃以上的温度下容易失活。蛋白P5对几种革兰氏阴性细菌有活性，但没有检测到对革兰氏阳性菌的活性。细胞壁酶切分析表明P5不是糖苷酶，而是一种内肽酶，它能裂解内消旋二氨基庚二酸和D-丙氨酸形成的肽桥。
The lytic enzyme of the lipid-containing bacteriophage phi6, protein P5, has been purified to apparent homogeneity from disrupted viral particles. The enzyme is a monomer with a molecular mass of approx. 24 kDa. The optimal pH for P5 activity is 8.5 and the protein is readily inactivated at temperatures above 20-degrees-C. Protein P5 is active against several Gram-negative bacteria, but no activity against Gram-positive species was detected. Analysis of cell wall digests indicates that P5 is not a glycosidase, but an endopeptidase splitting the peptide bridge formed by meso-diaminopimelic acid and D-alanine.